Compositions comprising polypeptides having xylanase activity and polypeptides having arabinofuranosidase activity

ABSTRACT

Compositions comprising polypeptides having xylanase activity and polypeptides having arabinofuranosidase activity for use in e.g. animal feed. Polypeptides having arabinofuranosidase activity, polypeptides having xylanase activity and polynucleotides encoding the polypeptides. Nucleic acid constructs, vectors, and host cells comprising the polynucleotides as well as methods of producing and using the polypeptide.

CROSS-REFERENCE TO RELATED APPLICATIONS

This application is a 35 U.S.C. 371 national application ofinternational application no. PCT/CN2015/097895 filed Dec. 18, 2015,which claims priority or the benefit under 35 U.S.C. 119 ofInternational application nos. PCT/CN2014/094381 and PCT/CN2015/071015filed Dec. 19, 2014 and Jan. 19, 2015, respectively. The content ofthese application is fully incorporated herein by reference.

REFERENCE TO A SEQUENCE LISTING

This application contains a Sequence Listing in computer readable form,which is incorporated herein by reference.

BACKGROUND OF THE INVENTION Field of the Invention

The present invention relates to compositions comprising polypeptideshaving xylanase activity and polypeptides having arabinofuranosidaseactivity for use in e.g. animal feed. The present invention furtherrelates to polypeptides having arabinofuranosidase activity,polypeptides having xylanase activity and polynucleotides encoding thepolypeptides. The invention also relates to nucleic acid constructs,vectors, and host cells comprising the polynucleotides as well asmethods of producing and using the polypeptides.

Description of the Related Art

Xylans are hemicelluloses found in all land plants (Popper and Tuohy,Plant Physiology, 2010, 153:373-383). They are especially abundant insecondary cell walls and xylem cells. In grasses, with type II cellwalls, glucurono arabinoxylans are the main hemicellulose and arepresent as soluble or insoluble dietary fiber in many grass based foodand feed products.

Plant xylans have a β-1,4-linked xylopyranose backbone that can besubstituted at the O2 or O3 position with arabinose,4-O-methyl-glucuronic acid, glucuronic acid and acetic acid in a speciesand tissue specific manner. The starch-rich seeds of the Panicoideaewith economically important species such as corn and sorghum havespecial types of highly substituted xylans in their cell walls. Comparedto wheat flour, wherein over 60% of the xylosyl units in thearabinoxylan backbone are unsubstituted, the corresponding percentage ofunsubstituted backbone xylosyls is 20-30% in corn kernel xylan, and35-40% in sorghum (Huismann et al. Carbohydrate Polymers, 2000,42:269-279). Furthermore, in corn and sorghum the xylan side chains canbe longer than a single arabinose or glucuronic acid substitution whichis typical of other xylans. This added side chain complexity is oftendue to L- and D-galactose and D-xylose sugars bound to the side chainarabinose or (4-O-methyl)-glucuronic acid. About every eleventharabinose in corn kernel xylan is also esterified with a ferulic acidand about every fifth xylose carries an acetylation (Agger et al. J.Agric. Food Chem, 2010, 58:6141-6148). All of these factors combinedmake the highly substituted xylans in corn and sorghum resistant todegradation by traditional xylanases.

The known enzymes responsible for the hydrolysis of carbohydrate basedpolymers are classified into enzyme families based on sequencesimilarity (www.cazy.org). The enzymes within a family share somecharacteristics such as 3D fold and they usually share the same reactionmechanism. Some GH families have narrow or mono-specific substratespecificities while other families have broad substrate specificities.The enzymes with mainly endo-xylanase activity have previously beendescribed in glycoside hydrolase family (GH) 5, 8, 10, 11 and 30. Theenzymes with mainly alpha-arabinofuranosidase activity have previouslybeen described in glycoside hydrolase family (GH) 3, 43, 51, 54 and 62.

Commercially available GH10 and GH11 xylanases are often used to breakdown the xylose backbone of arabinoxylan. In animal feed this results ina degradation of the cereal cell wall with a subsequent improvement innutrient release (starch and protein) encapsulated within the cells.Degradation of xylan also results in the formation of xylose oligomersthat may be utilised for hind gut fermentation and therefore helps ananimal to obtain more digestible energy. However, such xylanases aresensitive to side chain steric hindrance and whilst they are effectiveat degrading arabinoxylan from wheat, they are not very effective on thearabinoxylan found in the seeds of Panicoideae species, such as corn orsorghum.

WO2009/108941 suggests the use of over 500 different polypeptidesequences with many activities, such as cellulase, ligninase, betaglucosidase, hemicellulase, xylanase, alpha-amylase, amyloglucosidase,pectate lyase, cutinase, lipase, pectolyase, or maltogenic alpha amylaseactivity in a multitude of different applications. WO2009/018537suggests the use of a number of glycosyl hydrolases having differentactivities and ferulic acid esterases for convert lignocellulosicbiomass to fermentable sugar. WO2013/182669 discloses a number ofglycosyl hydrolases having different activities from Myriococcumthermophilum strain CBS 389.93 and the use in biomass processing.WO2009/108941 suggests the use of yeast strains secreting multipleenzymes of different activities for biomass hydrolysis.

Corn is used around the world in animal feed and thus there is a need todiscover new solutions that are capable of breaking down the highlybranched xylan backbone in the cell wall in order to release more xyloseand other nutrients which are trapped inside the cell wall.

SUMMARY OF THE INVENTION

The present invention relates to compositions comprising one or moreGH10 or GH11 polypeptides having xylanase activity and one or more GH62polypeptides having arabinofuranosidase activity, wherein:

-   -   (a) the GH62 polypeptide comprises the motif        [H/Y][L/M]F[F/S][A/C/H/S/T/V][A/D/G/N/R]D[D/E/N]G (SEQ ID NO:        1);    -   (b) the GH10 or GH11 polypeptide and the GH62 polypeptide        together solubilise at least 2.0% xylose from defatted        destarched maize (DFDSM); and    -   (c) the GH10 or GH11 polypeptide and the GH62 polypeptide        together solubilise at least 2 times more xylose from DFDSM than        the GH10 or GH11 polypeptide can when the GH62 polypeptide is        not present;    -   wherein (b) and (c) are performed under the reaction conditions:        -   i) 25 mg GH10 or GH11 polypeptide per kg DFDSM,        -   ii) 12.5 mg GH62 polypeptide per kg DFDSM, and        -   iii) incubation at 40° C., pH 5 for 4 hours.

The present application further relates to isolated polypeptides havingarabinofuranosidase activity, isolated polypeptides having xylanaseactivity, compositions comprising polypeptides havingarabinofuranosidase activity and/or xylanase activity, animal feed andanimal feed additives comprising the polypeptide(s) of the invention,methods of improving the performance of an animal comprisingadministering to the animal the composition of the invention; methodsfor improving the nutritional value of an animal feed comprisingadministering to the animal the composition of the invention; methods ofsolubilising xylose from plant based material, comprising treating plantbased material from the sub-family Panicoideae with the composition ofthe invention; methods of releasing starch from plant based material,comprising treating plant based material from the sub-family Panicoideaewith the composition of the invention; methods for improving thenutritional value of an animal feed, comprising adding to the feed thecomposition of the invention; methods of preparing an animal feed,comprising mixing the composition of the invention with plant basedmaterial from the sub-family Panicoideae; use of the composition of theinvention in animal feed, in animal feed additives, in the preparationof a composition for use in animal feed, for improving the nutritionalvalue of an animal feed, for increasing digestibility of the animalfeed, for improving one or more performance parameters in an animal, forreleasing xylose from plant based material of the sub-familyPanicoideae, and/or for releasing starch from plant based material ofthe sub-family Panicoideae, polynucleotides encoding the polypeptides ofthe present invention; nucleic acid constructs; expression vectors;recombinant host cells comprising the polynucleotides; and methods ofproducing the polypeptides.

Overview of Sequence Listing

SEQ ID NO: 1 is the GH62 conserved motif:[H/Y][L/M]F[F/S][A/C/H/S/T/V][A/D/G/N/R]D[D/E/N]G.

SEQ ID NO: 2 is the GH62 conserved motif: [H/Y]LF[F/S][A/S/V][A/D/G]DNG

SEQ ID NO: 3 is the GH62 conserved motif: YLFF[A/V][A/G]DNG

SEQ ID NO: 4 is the GH62 conserved motif: YLFFAGDNG

SEQ ID NO: 5 is the GH62 conserved motif: [H/Y]LFSSDDNG

SEQ ID NO: 6 is the GH62 conserved motif: YLFSSDDNG

SEQ ID NO: 7 is the gene sequence of GH62 arabinofuranosidase asisolated from Penicillium capsulatum.

SEQ ID NO: 8 is the amino acid sequence as deduced from SEQ ID NO: 7 andas disclosed as SEQ ID NO: 2 in WO2006/125438.

SEQ ID NO: 9 is the amino acid sequence of the mature GH62arabinofuranosidase from Penicillium capsulatum.

SEQ ID NO: 10 is the gene sequence of GH62 arabinofuranosidase asisolated from Penicillium aurantiogriseum.

SEQ ID NO: 11 is the amino acid sequence as deduced from SEQ ID NO: 10.

SEQ ID NO: 12 is the amino acid sequence of the mature GH62arabinofuranosidase from Penicillium aurantiogriseum.

SEQ ID NO: 13 is the codon optimised DNA sequence of the gene sequenceUniprot:XM_001273614 which is a GH62 arabinofuranosidase isolated fromAspergillus clavatus.

SEQ ID NO: 14 is the amino acid sequence as deduced from SEQ ID NO: 13(Uniprot:A1CCD2) and as disclosed as SEQ ID NO: 996 in WO2014/081884.

SEQ ID NO: 15 is the amino acid sequence of the mature GH62arabinofuranosidase from Aspergillus clavatus.

SEQ ID NO: 16 is the codon optimised DNA sequence of the gene sequenceUniprot:XM_001265651 which is a GH62 arabinofuranosidase isolated fromNeosartorya fischeri.

SEQ ID NO: 17 is the amino acid sequence as deduced from SEQ ID NO: 16(Uniprot:A1CYD5) and as disclosed as SEQ ID NO: 1177 in WO2014/081884.

SEQ ID NO: 18 is the amino acid sequence of the mature GH62arabinofuranosidase from Neosartorya fischeri.

SEQ ID NO: 19 is the codon optimised DNA sequence of the gene sequenceUniprot:XM_755363 which is a GH62 arabinofuranosidase isolated fromUstilago maydis (see Kaemper et al, Nature, 2006, 444, 97-101).

SEQ ID NO: 20 is the amino acid sequence as deduced from SEQ ID NO: 19(Uniprot:Q4P6F4).

SEQ ID NO: 21 is the amino acid sequence of the mature GH62arabinofuranosidase from Ustilago maydis.

SEQ ID NO: 22 is the gene sequence of GH62 arabinofuranosidase asisolated from Penicillium oxalicum.

SEQ ID NO: 23 is the amino acid sequence as deduced from SEQ ID NO: 22.

SEQ ID NO: 24 is the amino acid sequence of the mature GH62arabinofuranosidase from Penicillium oxalicum.

SEQ ID NO: 25 is the gene sequence of GH62 arabinofuranosidase asisolated from Talaromyces pinophilus.

SEQ ID NO: 26 is the amino acid sequence as deduced from SEQ ID NO: 25.

SEQ ID NO: 27 is the amino acid sequence of the mature GH62arabinofuranosidase from Talaromyces pinophilus.

SEQ ID NO: 28 is the gene sequence of GH62 arabinofuranosidase asisolated from Streptomyces nitrosporeus.

SEQ ID NO: 29 is the amino acid sequence as deduced from SEQ ID NO: 28.

SEQ ID NO: 30 is the amino acid sequence of the mature GH62arabinofuranosidase from Streptomyces nitrosporeus.

SEQ ID NO: 31 is the DNA sequence of the recombinant expressed DNAsequence from SEQ ID NO: 28 with His-tag and Savinase signal peptide.

SEQ ID NO: 32 is the amino acid sequence as deduced from SEQ ID NO: 31.

SEQ ID NO: 33 is the amino acid sequence of the mature GH62arabinofuranosidase obtained from SEQ ID NO. 32.

SEQ ID NO: 34 is the gene sequence of GH62 arabinofuranosidase asisolated from Streptomyces beijiangensis.

SEQ ID NO: 35 is the amino acid sequence as deduced from SEQ ID NO: 34.

SEQ ID NO: 36 is the amino acid sequence of the mature GH62arabinofuranosidase from Streptomyces beijiangensis.

SEQ ID NO: 37 is the DNA sequence of the recombinant expressed DNAsequence from SEQ ID NO: 34 with His-tag and Savinase signal peptide.

SEQ ID NO: 38 is the amino acid sequence as deduced from SEQ ID NO: 37.

SEQ ID NO: 39 is the amino acid sequence of the mature GH62arabinofuranosidase obtained from SEQ ID NO. 38.

SEQ ID NO: 40 is the gene sequence of GH62 arabinofuranosidase asisolated from Aspergillus clavatus (see Fedorova et al, PLoS, 100046).

SEQ ID NO: 41 is the amino acid sequence as deduced from SEQ ID NO: 40.

SEQ ID NO: 42 is the amino acid sequence of the mature GH62arabinofuranosidase from Aspergillus clavatus.

SEQ ID NO: 43 is the DNA sequence of the recombinant expressed DNAsequence from SEQ ID NO: 40 with His-tag.

SEQ ID NO: 44 is the amino acid sequence as deduced from SEQ ID NO: 43.

SEQ ID NO: 45 is the amino acid sequence of the mature GH62arabinofuranosidase obtained from SEQ ID NO. 44.

SEQ ID NO: 46 is the gene sequence of GH62 arabinofuranosidase asisolated from Aspergillus wentii.

SEQ ID NO: 47 is the amino acid sequence as deduced from SEQ ID NO: 46.

SEQ ID NO: 48 is the amino acid sequence of the mature GH62arabinofuranosidase from Aspergillus wentii.

SEQ ID NO: 49 is the DNA sequence of the recombinant expressed DNAsequence from SEQ ID NO: 46 with His-tag.

SEQ ID NO: 50 is the amino acid sequence as deduced from SEQ ID NO: 49.

SEQ ID NO: 51 is the amino acid sequence of the mature GH62arabinofuranosidase obtained from SEQ ID NO. 50.

SEQ ID NO: 52 is the gene sequence of GH62 arabinofuranosidase asisolated from Acrophialophora fusispora.

SEQ ID NO: 53 is the amino acid sequence as deduced from SEQ ID NO: 52.

SEQ ID NO: 54 is the amino acid sequence of the mature GH62arabinofuranosidase from Acrophialophora fusispora.

SEQ ID NO: 55 is the DNA sequence of the recombinant expressed DNAsequence from SEQ ID NO: 52 with His-tag.

SEQ ID NO: 56 is the amino acid sequence as deduced from SEQ ID NO: 55.

SEQ ID NO: 57 is the amino acid sequence of the mature GH62arabinofuranosidase obtained from SEQ ID NO. 56.

SEQ ID NO: 58 is the gene sequence of GH62 arabinofuranosidase asisolated from Streptosporangium sp-60756.

SEQ ID NO: 59 is the amino acid sequence as deduced from SEQ ID NO: 58.

SEQ ID NO: 60 is the amino acid sequence of the mature GH62arabinofuranosidase from Streptosporangium sp-60756.

SEQ ID NO: 61 is the DNA sequence of the recombinant expressed DNAsequence from SEQ ID NO: 58 with His-tag and Savinase signal peptide.

SEQ ID NO: 62 is the amino acid sequence as deduced from SEQ ID NO: 61.

SEQ ID NO: 63 is the amino acid sequence of the mature GH62arabinofuranosidase obtained from SEQ ID NO. 62.

SEQ ID NO: 64 is the gene sequence of GH62 arabinofuranosidase asisolated from Acrophialophora fusispora.

SEQ ID NO: 65 is the amino acid sequence as deduced from SEQ ID NO: 64.

SEQ ID NO: 66 is the amino acid sequence of the mature GH62arabinofuranosidase from Acrophialophora fusispora.

SEQ ID NO: 67 is the DNA sequence of the recombinant expressed DNAsequence from SEQ ID NO: 64 with His-tag.

SEQ ID NO: 68 is the amino acid sequence as deduced from SEQ ID NO: 67.

SEQ ID NO: 69 is the amino acid sequence of the mature GH62arabinofuranosidase obtained from SEQ ID NO. 68.

SEQ ID NO: 70 is the amino acid sequence of the mature GH10 xylanasefrom Aspergillus aculeatus as disclosed as SEQ ID NO: 5 (Xyl II) in WO1994/021785.

SEQ ID NO: 71 is the amino acid sequence of the mature GH10 xylanasefrom Clostridium acetobutylicum (Swissprot Q97TP5).

SEQ ID NO: 72 is the amino acid sequence of the mature GH10 xylanasefrom Aspergillus aculeatus as disclosed as SEQ ID NO: 8 in WO2005/059084.

SEQ ID NO: 73 is the amino acid sequence of the mature GH11 xylanasefrom Thermomyces lanuginosus as disclosed as SEQ ID NO: 2 ofWO1996/23062.

SEQ ID NO: 74 is the amino acid sequence of the mature GH11 xylanasefrom Dictyoglomus thermophilum as disclosed as SEQ ID NO: 305 ofWO2011/057140.

SEQ ID NO: 75 is the amino acid sequence of the mature GH11 xylanasefrom Paenibacillus pabuli as disclosed as SEQ ID NO: 2 of WO2005/079585.

SEQ ID NO: 76 is the gene sequence of a GH11 xylanase as isolated fromGeobacillus stearothermophilus.

SEQ ID NO: 77 is the amino acid sequence as deduced from SEQ ID NO: 76(Swissprot: P45705).

SEQ ID NO: 78 is the amino acid sequence of the mature GH11 xylanasefrom Geobacillus stearothermophilus.

SEQ ID NO: 79 is the DNA sequence of the synthetic DNA sequence from SEQID NO: 76 with Savinase signal peptide.

SEQ ID NO: 80 is the amino acid sequence as deduced from SEQ ID NO: 79.

SEQ ID NO: 81 is the amino acid sequence of the mature GH11 xylanaseobtained from SEQ ID NO. 80.

SEQ ID NO: 82 is the gene sequence of a GH11 xylanase as isolated fromStreptomyces beijiangensis.

SEQ ID NO: 83 is the amino acid sequence as deduced from SEQ ID NO: 88.

SEQ ID NO: 84 is the amino acid sequence of the mature GH11 xylanasefrom Streptomyces beijiangensis.

SEQ ID NO: 85 is the DNA sequence of the recombinant expressed DNAsequence from SEQ ID NO: 82 with His-tag and Savinase signal peptide.

SEQ ID NO: 86 is the amino acid sequence as deduced from SEQ ID NO: 85.

SEQ ID NO: 87 is the amino acid sequence of the mature GH62arabinofuranosidase obtained from SEQ ID NO: 86.

SEQ ID NO: 88 is the amino acid sequence of the mature GH11 xylanasefrom Fusarium oxysporum (FoxXyn 6) as disclosed as SEQ ID NO: 8 inWO2014/019220.

SEQ ID NO: 89 is the amino acid sequence of the mature GH11 xylanasefrom Aspergillus clavatus (AcIXyn5) as disclosed as SEQ ID NO: 8 inWO2014/020143.

SEQ ID NO: 90 is the Bacillus lentus secretion signal.

SEQ ID NO: 91 is the His-tag RHHHHHHP.

SEQ ID NO: 92 is the His-tag HHHHHHPR.

SEQ ID NO: 93 is the amino acid sequence of the GH43 arabinofuranosidasefrom Humicola insolens as disclosed as SEQ ID NO: 1 in WO2006/114095.

SEQ ID NO: 94 is the amino acid sequence of the GH51 arabinofuranosidasefrom Meripilus giganteus as disclosed as SEQ ID NO: 2 in WO2006/114095.

SEQ ID NO: 95 is the amino acid sequence of the mature GH10 xylanaseXynB from Thermotoga maritima MSB8 as disclosed as SEQ ID NO: 1 ofWO2013/068550.

SEQ ID NO: 96 is the amino acid sequence of the mature GH11 xylanaseXyl6 from Myceliophthora thermophila as disclosed as SEQ ID NO: 41 ofWO2009/018537.

SEQ ID NO: 97 is the gene sequence of a GH11 xylanase as isolated fromLasiodiplodia theobromae.

SEQ ID NO: 98 is the amino acid sequence as deduced from SEQ ID NO: 97.

SEQ ID NO: 99 is the amino acid sequence of the mature GH11 xylanasefrom Lasiodiplodia theobromae.

SEQ ID NO: 100 is the gene sequence of a GH10 xylanase as isolated fromAscobolus stictoideus.

SEQ ID NO: 101 is the amino acid sequence as deduced from SEQ ID NO:100.

SEQ ID NO: 102 is the amino acid sequence of the mature GH10 xylanasefrom Ascobolus stictoideus.

SEQ ID NO: 103 is the gene sequence of GH62 arabinofuranosidase asisolated from Drechslera sp.

SEQ ID NO: 104 is the amino acid sequence as deduced from SEQ ID NO:104.

SEQ ID NO: 105 is the amino acid sequence of the mature GH62arabinofuranosidase from Drechslera sp.

SEQ ID NO: 106 is the gene sequence of GH62 arabinofuranosidase asisolated from Xylanibacterium sp-61981.

SEQ ID NO: 107 is the amino acid sequence as deduced from SEQ ID NO:106.

SEQ ID NO: 108 is the amino acid sequence of the mature GH62arabinofuranosidase from Xylanibacterium sp-61981.

SEQ ID NO: 109 is the DNA sequence of the recombinant expressed DNAsequence from SEQ ID NO: 106 with His-tag.

SEQ ID NO: 110 is the amino acid sequence as deduced from SEQ ID NO:109.

SEQ ID NO: 111 is the amino acid sequence of the mature GH62arabinofuranosidase obtained from SEQ ID NO. 110.

SEQ ID NO: 112 is the gene sequence of GH62 arabinofuranosidase asisolated from Microdochium nivale.

SEQ ID NO: 113 is the amino acid sequence as deduced from SEQ ID NO:112.

SEQ ID NO: 114 is the amino acid sequence of the mature GH62arabinofuranosidase from Microdochium nivale.

SEQ ID NO: 115 is the DNA sequence of the recombinant expressed DNAsequence from SEQ ID NO: 112 with His-tag.

SEQ ID NO: 116 is the amino acid sequence as deduced from SEQ ID NO:115.

SEQ ID NO: 117 is the amino acid sequence of the mature GH62arabinofuranosidase obtained from SEQ ID NO. 116.

SEQ ID NO: 118 is the gene sequence of GH62 arabinofuranosidase asisolated from Humicola hyalothermophila.

SEQ ID NO: 119 is the amino acid sequence as deduced from SEQ ID NO:118.

SEQ ID NO: 120 is the amino acid sequence of the mature GH62arabinofuranosidase from Humicola hyalothermophila.

SEQ ID NO: 121 is the gene sequence of GH62 arabinofuranosidase asisolated from Curvularia geniculata.

SEQ ID NO: 122 is the amino acid sequence as deduced from SEQ ID NO:121.

SEQ ID NO: 123 is the amino acid sequence of the mature GH62arabinofuranosidase from Curvularia geniculata.

SEQ ID NO: 124 is the gene sequence of GH62 arabinofuranosidase asisolated from Glycomyces rutgersensis.

SEQ ID NO: 125 is the amino acid sequence as deduced from SEQ ID NO:124.

SEQ ID NO: 126 is the amino acid sequence of the mature GH62arabinofuranosidase from Glycomyces rutgersensis.

SEQ ID NO: 127 is the DNA sequence of the recombinant expressed DNAsequence from SEQ ID NO: 124 with His-tag and Savinase signal peptide.

SEQ ID NO: 128 is the amino acid sequence as deduced from SEQ ID NO:127.

SEQ ID NO: 129 is the amino acid sequence of the mature GH62arabinofuranosidase obtained from SEQ ID NO. 128.

SEQ ID NO: 130 is the gene sequence of GH62 arabinofuranosidase asisolated from Coprinopsis cinerea as disclosed in Proc Natl Acad SciUSA, 2010 107:11889-11894 and Biosci Biotechnol Biochem. 201075:342-345.

SEQ ID NO: 131 is the amino acid sequence as deduced from SEQ ID NO:130.

SEQ ID NO: 132 is the amino acid sequence of the mature GH62arabinofuranosidase from Coprinopsis cinerea.

SEQ ID NO: 133 is the DNA sequence of the recombinant expressed DNAsequence from SEQ ID NO: 130 with His-tag.

SEQ ID NO: 134 is the amino acid sequence as deduced from SEQ ID NO:133.

SEQ ID NO: 135 is the amino acid sequence of the mature GH62arabinofuranosidase obtained from SEQ ID NO. 134.

SEQ ID NO: 136 is the gene sequence of GH62 arabinofuranosidase asisolated from Aspergillus aculeatus.

SEQ ID NO: 137 is the amino acid sequence as deduced from SEQ ID NO:136.

SEQ ID NO: 138 is the amino acid sequence of the mature GH62arabinofuranosidase from Aspergillus aculeatus.

SEQ ID NO: 139 is the gene sequence of GH62 arabinofuranosidase asisolated from Remersonia thermophila.

SEQ ID NO: 140 is the amino acid sequence as deduced from SEQ ID NO:139.

SEQ ID NO: 141 is the amino acid sequence of the mature GH62arabinofuranosidase from Remersonia thermophila.

SEQ ID NO: 142 is the DNA sequence of the recombinant expressed DNAsequence from SEQ ID NO: 139 with His-tag.

SEQ ID NO: 143 is the amino acid sequence as deduced from SEQ ID NO:142.

SEQ ID NO: 144 is the amino acid sequence of the mature GH62arabinofuranosidase obtained from SEQ ID NO. 143.

SEQ ID NO: 145 is the gene sequence of GH62 arabinofuranosidase asisolated from Penicillium soppii.

SEQ ID NO: 155 is the amino acid sequence as deduced from SEQ ID NO:145.

SEQ ID NO: 147 is the amino acid sequence of the mature GH62arabinofuranosidase from Penicillium soppii.

SEQ ID NO: 148 is the gene sequence of GH62 arabinofuranosidase asisolated from Bipolaris sorokiniana.

SEQ ID NO: 149 is the amino acid sequence as deduced from SEQ ID NO:148.

SEQ ID NO: 150 is the amino acid sequence of the mature GH62arabinofuranosidase from Bipolaris sorokiniana.

SEQ ID NO: 151 is the DNA sequence of the recombinant expressed DNAsequence from SEQ ID NO: 148 with His-tag.

SEQ ID NO: 152 is the amino acid sequence as deduced from SEQ ID NO:151.

SEQ ID NO: 153 is the amino acid sequence of the mature GH62arabinofuranosidase obtained from SEQ ID NO. 152.

SEQ ID NO: 154 is the gene sequence of GH62 arabinofuranosidase asisolated from Aspergillus fumigatiaffinis.

SEQ ID NO: 155 is the amino acid sequence as deduced from SEQ ID NO:154.

SEQ ID NO: 156 is the amino acid sequence of the mature GH62arabinofuranosidase from Aspergillus fumigatiaffinis.

SEQ ID NO: 157 is the gene sequence of GH62 arabinofuranosidase asisolated from Neosartorya fischeri as disclosed in “Genomic islands inthe pathogenic filamentous fungus Aspergillus fumigatus,” PLoS. DOI:10.1371/journal.pgen.1000046.

SEQ ID NO: 158 is the amino acid sequence as deduced from SEQ ID NO:157.

SEQ ID NO: 159 is the amino acid sequence of the mature GH62arabinofuranosidase from Neosartorya fischeri.

SEQ ID NO: 160 is the gene sequence of GH62 arabinofuranosidase asisolated from Thielavia arenaria.

SEQ ID NO: 161 is the amino acid sequence as deduced from SEQ ID NO:160.

SEQ ID NO: 162 is the amino acid sequence of the mature GH62arabinofuranosidase from Thielavia arenaria.

SEQ ID NO: 163 is the gene sequence of GH62 arabinofuranosidase asisolated from Chaetomium olivicolor.

SEQ ID NO: 164 is the amino acid sequence as deduced from SEQ ID NO:163.

SEQ ID NO: 165 is the amino acid sequence of the mature GH62arabinofuranosidase from Chaetomium olivicolor.

SEQ ID NO: 166 is the gene sequence of GH62 arabinofuranosidase asisolated from Thielavia terricola.

SEQ ID NO: 167 is the amino acid sequence as deduced from SEQ ID NO:166.

SEQ ID NO: 168 is the amino acid sequence of the mature GH62arabinofuranosidase from Thielavia terricola.

SEQ ID NO: 169 is the gene sequence of GH62 arabinofuranosidase asisolated from Thielavia terricola.

SEQ ID NO: 170 is the amino acid sequence as deduced from SEQ ID NO:169.

SEQ ID NO: 171 is the amino acid sequence of the mature GH62arabinofuranosidase from Thielavia terricola.

SEQ ID NO: 172 is the gene sequence of GH62 arabinofuranosidase asisolated from Humicola sp.

SEQ ID NO: 173 is the amino acid sequence as deduced from SEQ ID NO:172.

SEQ ID NO: 174 is the amino acid sequence of the mature GH62arabinofuranosidase from Humicola sp.

SEQ ID NO: 175 is the gene sequence of a GH10 xylanase as isolated fromUstilago maydis as disclosed in Nature, 2006 444:97-101.

SEQ ID NO: 176 is the amino acid sequence as deduced from SEQ ID NO:175.

SEQ ID NO: 177 is the amino acid sequence of the mature GH10 xylanasefrom Ustilago maydis

SEQ ID NO: 178 is the DNA sequence of the recombinant expressed DNAsequence from SEQ ID NO: 175 with His-tag.

SEQ ID NO: 179 is the amino acid sequence as deduced from SEQ ID NO:178.

SEQ ID NO: 180 is the amino acid sequence of the mature GH10 xylanaseobtained from SEQ ID NO: 179.

Definitions

Allelic variant: The term “allelic variant” means any of two or morealternative forms of a gene occupying the same chromosomal locus.Allelic variation arises naturally through mutation, and may result inpolymorphism within populations. Gene mutations can be silent (no changein the encoded polypeptide) or may encode polypeptides having alteredamino acid sequences. An allelic variant of a polypeptide is apolypeptide encoded by an allelic variant of a gene.

Arabinofuranosidase: The term “arabinofuranosidase” means analpha-L-arabinofuranoside arabinofuranohydrolase (EC 3.2.1.55) thatcatalyzes the hydrolysis of terminal non-reducingalpha-L-arabinofuranoside residues in alpha-L-arabinosides. The enzymeacts on alpha-L-arabinofuranosides, alpha-L-arabinans containing (1,3)-and/or (1,2)- and/or (1,5)-linkages, arabinoxylans, andarabinogalactans. Alpha-L-arabinofuranosidase is also known asarabinosidase, alpha-arabinosidase, alpha-L-arabinosidase,alpha-arabinofuranosidase, polysaccharide alpha-L-arabinofuranosidase,alpha-L-arabinofuranoside hydrolase, L-arabinosidase, oralpha-L-arabinanase. Arabinofuranosidase activity can be determinedusing 5 mg of medium viscosity wheat arabinoxylan (MegazymeInternational Ireland, Ltd., Bray, Co. Wicklow, Ireland) per ml of 100mM sodium acetate pH 5 in a total volume of 200 μl for 30 minutes at 40°C. followed by arabinose analysis by AMINEX® HPX-87H columnchromatography (Bio-Rad Laboratories, Inc., Hercules, Calif., USA).

The arabinofuranosidase of the present invention have at least 50% ofthe arabinofuranosidase activity of one or more of the polypeptidesselected from the list consisting of SEQ ID NO: 9, SEQ ID NO: 12, SEQ IDNO: 15, SEQ ID NO: 18, SEQ ID NO: 21, SEQ ID NO: 24, SEQ ID NO: 27, SEQID NO: 30, SEQ ID NO: 33, SEQ ID NO: 36, SEQ ID NO: 39, SEQ ID NO: 42,SEQ ID NO: 45, SEQ ID NO: 48, SEQ ID NO: 51, SEQ ID NO: 54, SEQ ID NO:57, SEQ ID NO: 60, SEQ ID NO: 63, SEQ ID NO: 66, SEQ ID NO: 69, SEQ IDNO: 105, SEQ ID NO: 108, SEQ ID NO: 111, SEQ ID NO: 114, SEQ ID NO: 117,SEQ ID NO: 120, SEQ ID NO: 123, SEQ ID NO: 126, SEQ ID NO: 129, SEQ IDNO: 132, SEQ ID NO: 135, SEQ ID NO: 138, SEQ ID NO: 141, SEQ ID NO: 144,SEQ ID NO: 147, SEQ ID NO: 150, SEQ ID NO: 153, SEQ ID NO: 156, SEQ IDNO: 159, SEQ ID NO: 162, SEQ ID NO: 165, SEQ ID NO: 168, SEQ ID NO: 171and SEQ ID NO: 174. In a preferred embodiment, the arabinofuranosidaseof the present invention have at least 70% of the arabinofuranosidaseactivity of one or more of the polypeptides selected from the listconsisting of SEQ ID NO: 9, SEQ ID NO: 12, SEQ ID NO: 15, SEQ ID NO: 18,SEQ ID NO: 21, SEQ ID NO: 24, SEQ ID NO: 27, SEQ ID NO: 30, SEQ ID NO:33, SEQ ID NO: 36, SEQ ID NO: 39, SEQ ID NO: 42, SEQ ID NO: 45, SEQ IDNO: 48, SEQ ID NO: 51, SEQ ID NO: 54, SEQ ID NO: 57, SEQ ID NO: 60, SEQID NO: 63, SEQ ID NO: 66, SEQ ID NO: 69, SEQ ID NO: 105, SEQ ID NO: 108,SEQ ID NO: 111, SEQ ID NO: 114, SEQ ID NO: 117, SEQ ID NO: 120, SEQ IDNO: 123, SEQ ID NO: 126, SEQ ID NO: 129, SEQ ID NO: 132, SEQ ID NO: 135,SEQ ID NO: 138, SEQ ID NO: 141, SEQ ID NO: 144, SEQ ID NO: 147, SEQ IDNO: 150, SEQ ID NO: 153, SEQ ID NO: 156, SEQ ID NO: 159, SEQ ID NO: 162,SEQ ID NO: 165, SEQ ID NO: 168, SEQ ID NO: 171 and SEQ ID NO: 174. In apreferred embodiment, the arabinofuranosidase of the present inventionhave at least 80% of the arabinofuranosidase activity of one or more ofthe polypeptides selected from the list consisting of SEQ ID NO: 9, SEQID NO: 12, SEQ ID NO: 15, SEQ ID NO: 18, SEQ ID NO: 21, SEQ ID NO: 24,SEQ ID NO: 27, SEQ ID NO: 30, SEQ ID NO: 33, SEQ ID NO: 36, SEQ ID NO:39, SEQ ID NO: 42, SEQ ID NO: 45, SEQ ID NO: 48, SEQ ID NO: 51, SEQ IDNO: 54, SEQ ID NO: 57, SEQ ID NO: 60, SEQ ID NO: 63, SEQ ID NO: 66, SEQID NO: 69, SEQ ID NO: 105, SEQ ID NO: 108, SEQ ID NO: 111, SEQ ID NO:114, SEQ ID NO: 117, SEQ ID NO: 120, SEQ ID NO: 123, SEQ ID NO: 126, SEQID NO: 129, SEQ ID NO: 132, SEQ ID NO: 135, SEQ ID NO: 138, SEQ ID NO:141, SEQ ID NO: 144, SEQ ID NO: 147, SEQ ID NO: 150, SEQ ID NO: 153, SEQID NO: 156, SEQ ID NO: 159, SEQ ID NO: 162, SEQ ID NO: 165, SEQ ID NO:168, SEQ ID NO: 171 and SEQ ID NO: 174. In a preferred embodiment, thearabinofuranosidase of the present invention have at least 90% of thearabinofuranosidase activity of one or more of the polypeptides selectedfrom the list consisting of SEQ ID NO: 9, SEQ ID NO: 12, SEQ ID NO: 15,SEQ ID NO: 18, SEQ ID NO: 21, SEQ ID NO: 24, SEQ ID NO: 27, SEQ ID NO:30, SEQ ID NO: 33, SEQ ID NO: 36, SEQ ID NO: 39, SEQ ID NO: 42, SEQ IDNO: 45, SEQ ID NO: 48, SEQ ID NO: 51, SEQ ID NO: 54, SEQ ID NO: 57, SEQID NO: 60, SEQ ID NO: 63, SEQ ID NO: 66, SEQ ID NO: 69, SEQ ID NO: 105,SEQ ID NO: 108, SEQ ID NO: 111, SEQ ID NO: 114, SEQ ID NO: 117, SEQ IDNO: 120, SEQ ID NO: 123, SEQ ID NO: 126, SEQ ID NO: 129, SEQ ID NO: 132,SEQ ID NO: 135, SEQ ID NO: 138, SEQ ID NO: 141, SEQ ID NO: 144, SEQ IDNO: 147, SEQ ID NO: 150, SEQ ID NO: 153, SEQ ID NO: 156, SEQ ID NO: 159,SEQ ID NO: 162, SEQ ID NO: 165, SEQ ID NO: 168, SEQ ID NO: 171 and SEQID NO: 174. In a preferred embodiment, the arabinofuranosidase of thepresent invention have at least 95% of the arabinofuranosidase activityof one or more of the polypeptides selected from the list consisting ofSEQ ID NO: 9, SEQ ID NO: 12, SEQ ID NO: 15, SEQ ID NO: 18, SEQ ID NO:21, SEQ ID NO: 24, SEQ ID NO: 27, SEQ ID NO: 30, SEQ ID NO: 33, SEQ IDNO: 36, SEQ ID NO: 39, SEQ ID NO: 42, SEQ ID NO: 45, SEQ ID NO: 48, SEQID NO: 51, SEQ ID NO: 54, SEQ ID NO: 57, SEQ ID NO: 60, SEQ ID NO: 63,SEQ ID NO: 66, SEQ ID NO: 69, SEQ ID NO: 105, SEQ ID NO: 108, SEQ ID NO:111, SEQ ID NO: 114, SEQ ID NO: 117, SEQ ID NO: 120, SEQ ID NO: 123, SEQID NO: 126, SEQ ID NO: 129, SEQ ID NO: 132, SEQ ID NO: 135, SEQ ID NO:138, SEQ ID NO: 141, SEQ ID NO: 144, SEQ ID NO: 147, SEQ ID NO: 150, SEQID NO: 153, SEQ ID NO: 156, SEQ ID NO: 159, SEQ ID NO: 162, SEQ ID NO:165, SEQ ID NO: 168, SEQ ID NO: 171 and SEQ ID NO: 174.

In a preferred embodiment, the arabinofuranosidase of the presentinvention have at least 50%, such as at least 75%, at least 80%, atleast 85%, at least 90%, at least 95% or at least 100% of thearabinofuranosidase activity of SEQ ID NO: 111. In a preferredembodiment, the arabinofuranosidase of the present invention have atleast 50%, such as at least 75%, at least 80%, at least 85%, at least90%, at least 95% or at least 100% of the arabinofuranosidase activityof SEQ ID NO: 24.

Arabinoxylan-containing material: The term “Arabinoxylan-containingmaterial” means any material containing arabinoxylan. Arabinoxylan is ahemicellulose found in both the primary and secondary cell walls ofplants, including woods and cereal grains, consisting of copolymers oftwo pentose sugars, arabinose and xylose. The arabinoxylan chaincontains a large number of 1,4-linked xylose units. Many xylose unitsare substituted with 2-, 3- or 2,3-substituted arabinose residues.

Examples of arabinoxylan-containing material are forage, roughage, seedsand grains (either whole or prepared by crushing, milling, etc from e.g.corn, oats, rye, barley, wheat), trees or hard woods (such as poplar,willow, eucalyptus, palm, maple, birch), bamboo, herbaceous and/or woodyenergy crops, agricultural food and feed crops, animal feed products,cassava peels, cocoa pods, sugar cane, sugar beet, locust bean pulp,vegetable or fruit pomaces, wood waste, bark, shavings, sawdust, woodpulp, pulping liquor, waste paper, cardboard, construction anddemolition wood waste, industrial or municipal waste water solids orsludge, manure, by-product from brewing and/or fermentation processes,wet distillers grain, dried distillers grain, spent grain, vinasse andbagasse.

Forage as defined herein also includes roughage. Forage is fresh plantmaterial such as hay and silage from forage plants, grass and otherforage plants, grass and other forage plants, seaweed, sprouted grainsand legumes, or any combination thereof. Examples of forage plants areAlfalfa (Lucerne), birdsfoot trefoil, brassica (e.g. kale, rapeseed(canola), rutabaga (swede), turnip), clover (e.g. alsike clover, redclover, subterranean clover, white clover), grass (e.g. Bermuda grass,brome, false oat grass, fescue, heath grass, meadow grasses, miscanthus,orchard grass, ryegrass, switchgrass, Timothy-grass), corn (maize),hemp, millet, barley, oats, rye, sorghum, soybeans and wheat andvegetables such as beets. Crops suitable for ensilage are the ordinarygrasses, clovers, alfalfa, vetches, oats, rye and maize. Forage furtherincludes crop residues from grain production (such as corn stover; strawfrom wheat, barley, oat, rye and other grains); residues from vegetableslike beet tops; residues from oilseed production like stems and leavesform soy beans, rapeseed and other legumes; and fractions from therefining of grains for animal or human consumption or from fuelproduction or other industries.

Roughage is generally dry plant material with high levels of fiber, suchas fiber, bran, husks from seeds and grains and crop residues (such asstover, copra, straw, chaff, sugar beet waste).

Preferred sources of arabinoxylan-containing materials are forage,roughage, seeds and grains, sugar cane, sugar beet and wood pulp.

Body Weight Gain: The term “body weight gain” means an increase in liveweight of an animal during a given period of time e.g. the increase inweight from day 1 to day 21.

cDNA: The term “cDNA” means a DNA molecule that can be prepared byreverse transcription from a mature, spliced, mRNA molecule obtainedfrom a eukaryotic or prokaryotic cell. cDNA lacks intron sequences thatmay be present in the corresponding genomic DNA. The initial, primaryRNA transcript is a precursor to mRNA that is processed through a seriesof steps, including splicing, before appearing as mature spliced mRNA.

Coding sequence: The term “coding sequence” means a polynucleotide,which directly specifies the amino acid sequence of a polypeptide. Theboundaries of the coding sequence are generally determined by an openreading frame, which begins with a start codon such as ATG, GTG, or TTGand ends with a stop codon such as TAA, TAG, or TGA. The coding sequencemay be a genomic DNA, cDNA, synthetic DNA, or a combination thereof.

Control sequences: The term “control sequences” means nucleic acidsequences necessary for expression of a polynucleotide encoding a maturepolypeptide of the present invention. Each control sequence may benative (i.e., from the same gene) or foreign (i.e., from a differentgene) to the polynucleotide encoding the polypeptide or native orforeign to each other. Such control sequences include, but are notlimited to, a leader, polyadenylation sequence, propeptide sequence,promoter, signal peptide sequence, and transcription terminator. At aminimum, the control sequences include a promoter, and transcriptionaland translational stop signals. The control sequences may be providedwith linkers for the purpose of introducing specific restriction sitesfacilitating ligation of the control sequences with the coding region ofthe polynucleotide encoding a polypeptide.

Expression: The term “expression” includes any step involved in theproduction of a polypeptide including, but not limited to,transcription, post-transcriptional modification, translation,post-translational modification, and secretion.

Expression vector: The term “expression vector” means a linear orcircular DNA molecule that comprises a polynucleotide encoding apolypeptide and is operably linked to control sequences that provide forits expression.

Feed Conversion Ratio: The term “feed conversion ratio” the amount offeed fed to an animal to increase the weight of the animal by aspecified amount. An improved feed conversion ratio means a lower feedconversion ratio. By “lower feed conversion ratio” or “improved feedconversion ratio” it is meant that the use of a feed additivecomposition in feed results in a lower amount of feed being required tobe fed to an animal to increase the weight of the animal by a specifiedamount compared to the amount of feed required to increase the weight ofthe animal by the same amount when the feed does not comprise said feedadditive composition.

Feed efficiency: The term “feed efficiency” means the amount of weightgain per unit of feed when the animal is fed ad-libitum or a specifiedamount of food during a period of time. By “increased feed efficiency”it is meant that the use of a feed additive composition according thepresent invention in feed results in an increased weight gain per unitof feed intake compared with an animal fed without said feed additivecomposition being present.

Fragment: The term “fragment” means a polypeptide having one or more(e.g., several) amino acids absent from the amino and/or carboxylterminus of a mature polypeptide or domain; wherein the fragment hasarabinofuranosidase activity.

In one aspect, a fragment contains at least 90% of the amino acids ofthe mature polypeptide, such as 272 amino acids (SEQ ID NO: 8 or 9), 273amino acids (SEQ ID NO: 11 or 12), 344 amino acids (SEQ ID NO: 14 or15), 340 amino acids (SEQ ID NO: 17 or 18), 280 amino acids (SEQ ID NO:20 or 21), 272 amino acids (SEQ ID NO: 23 or 24), 278 amino acids (SEQID NO: 26 or 27), 394 amino acids (SEQ ID NO: 29 or 30), 401 amino acids(SEQ ID NO: 32 or 33), 394 amino acids (SEQ ID NO: 35 or 36), 401 aminoacids (SEQ ID NO: 38 or 39), 286 amino acids (SEQ ID NO: 41 or 42), 293amino acids (SEQ ID NO: 44 or 45), 272 amino acids (SEQ ID NO: 47 or48), 280 amino acids (SEQ ID NO: 50 or 51), 328 amino acids (SEQ ID NO:53 or 54), 336 amino acids (SEQ ID NO: 56 or 57), 392 amino acids (SEQID NO: 59 or 60), 400 amino acids (SEQ ID NO: 62 or 63), 272 amino acids(SEQ ID NO: 65 or 66), 280 amino acids (SEQ ID NO: 68 or 69), 346 aminoacids (SEQ ID NO: 70), 259 amino acids (SEQ ID NO: 71), 277 amino acids(SEQ ID NO: 72), 176 amino acids (SEQ ID NO: 73), 183 amino acids (SEQID NO: 74), 164 amino acids (SEQ ID NO: 75), 165 amino acids (SEQ ID NO:77 or 78), 163 amino acids (SEQ ID NO: 80 or 81), 269 amino acids (SEQID NO: 83 or 84), 276 amino acids (SEQ ID NO: 86 or 87), 169 amino acids(SEQ ID NO: 88), 170 amino acids (SEQ ID NO: 89), 183 amino acids (SEQID NO: 98 or 99), 304 amino acids (SEQ ID NO: 101 or 102), 272 aminoacids (SEQ ID NO: 104 or 105), 418 amino acids (SEQ ID NO: 107 or 108),328 amino acids (SEQ ID NO: 113 or 114), 322 amino acids (SEQ ID NO: 119or 120), 272 amino acids (SEQ ID NO: 122 or 123), 408 amino acids (SEQID NO: 125 or 126), 340 amino acids (SEQ ID NO: 131 or 132), 279 aminoacids (SEQ ID NO: 137 or 138), 274 amino acids (SEQ ID NO: 140 or 141),272 amino acids (SEQ ID NO: 146 or 147), 293 amino acids (SEQ ID NO: 148or 149), 272 amino acids (SEQ ID NO: 149 or 150), 285 amino acids (SEQID NO: 155 or 156), 285 amino acids (SEQ ID NO: 158 or 159), 273 aminoacids (SEQ ID NO: 161 or 162), 325 amino acids (SEQ ID NO: 164 or 165),336 amino acids (SEQ ID NO: 167 or 168), 272 amino acids (SEQ ID NO: 170or 171), 328 amino acids (SEQ ID NO: 173 or 174) or 291 amino acids (SEQID NO: 176 or 177).

In another aspect, a fragment contains at least 92% of the amino acidsof the mature polypeptide, such as 278 amino acids (SEQ ID NO: 8 or 9),279 amino acids (SEQ ID NO: 11 or 12), 351 amino acids (SEQ ID NO: 14 or15), 348 amino acids (SEQ ID NO: 17 or 18), 286 amino acids (SEQ ID NO:20 or 21), 278 amino acids (SEQ ID NO: 23 or 24), 284 amino acids (SEQID NO: 26 or 27), 403 amino acids (SEQ ID NO: 29 or 30), 410 amino acids(SEQ ID NO: 32 or 33), 403 amino acids (SEQ ID NO: 35 or 36), 410 aminoacids (SEQ ID NO: 38 or 39), 293 amino acids (SEQ ID NO: 41 or 42), 300amino acids (SEQ ID NO: 44 or 45), 278 amino acids (SEQ ID NO: 47 or48), 286 amino acids (SEQ ID NO: 50 or 51), 335 amino acids (SEQ ID NO:53 or 54), 343 amino acids (SEQ ID NO: 56 or 57), 401 amino acids (SEQID NO: 59 or 60), 408 amino acids (SEQ ID NO: 62 or 63), 278 amino acids(SEQ ID NO: 65 or 66), 286 amino acids (SEQ ID NO: 68 or 69), 353 aminoacids (SEQ ID NO: 70), 265 amino acids (SEQ ID NO: 71), 283 amino acids(SEQ ID NO: 72), 179 amino acids (SEQ ID NO: 73), 187 amino acids (SEQID NO: 74), 167 amino acids (SEQ ID NO: 75), 168 amino acids (SEQ ID NO:77 or 78), 167 amino acids (SEQ ID NO: 80 or 81), 275 amino acids (SEQID NO: 83 or 84), 282 amino acids (SEQ ID NO: 86 or 87), 173 amino acids(SEQ ID NO: 88), 174 amino acids (SEQ ID NO: 89), 187 amino acids (SEQID NO: 98 or 99), 311 amino acids (SEQ ID NO: 101 or 102), 278 aminoacids (SEQ ID NO: 104 or 105), 427 amino acids (SEQ ID NO: 107 or 108),335 amino acids (SEQ ID NO: 113 or 114), 329 amino acids (SEQ ID NO: 119or 120), 278 amino acids (SEQ ID NO: 122 or 123), 417 amino acids (SEQID NO: 125 or 126), 347 amino acids (SEQ ID NO: 131 or 132), 285 aminoacids (SEQ ID NO: 137 or 138), 280 amino acids (SEQ ID NO: 140 or 141),278 amino acids (SEQ ID NO: 146 or 147), 299 amino acids (SEQ ID NO: 148or 149), 278 amino acids (SEQ ID NO: 149 or 150), 291 amino acids (SEQID NO: 155 or 156), 291 amino acids (SEQ ID NO: 158 or 159), 279 aminoacids (SEQ ID NO: 161 or 162), 333 amino acids (SEQ ID NO: 164 or 165),344 amino acids (SEQ ID NO: 167 or 168), 278 amino acids (SEQ ID NO: 170or 171), 335 amino acids (SEQ ID NO: 173 or 174) or 298 amino acids (SEQID NO: 176 or 177).

In another aspect, a fragment contains at least 94% of the amino acidsof the mature polypeptide, such as 284 amino acids (SEQ ID NO: 8 or 9),285 amino acids (SEQ ID NO: 11 or 12), 359 amino acids (SEQ ID NO: 14 or15), 355 amino acids (SEQ ID NO: 17 or 18), 292 amino acids (SEQ ID NO:20 or 21), 284 amino acids (SEQ ID NO: 23 or 24), 290 amino acids (SEQID NO: 26 or 27), 412 amino acids (SEQ ID NO: 29 or 30), 419 amino acids(SEQ ID NO: 32 or 33), 412 amino acids (SEQ ID NO: 35 or 36), 419 aminoacids (SEQ ID NO: 38 or 39), 299 amino acids (SEQ ID NO: 41 or 42), 306amino acids (SEQ ID NO: 44 or 45), 284 amino acids (SEQ ID NO: 47 or48), 292 amino acids (SEQ ID NO: 50 or 51), 342 amino acids (SEQ ID NO:53 or 54), 351 amino acids (SEQ ID NO: 56 or 57), 410 amino acids (SEQID NO: 59 or 60), 417 amino acids (SEQ ID NO: 62 or 63), 284 amino acids(SEQ ID NO: 65 or 66), 292 amino acids (SEQ ID NO: 68 or 69), 361 aminoacids (SEQ ID NO: 70), 271 amino acids (SEQ ID NO: 71), 290 amino acids(SEQ ID NO: 72), 183 amino acids (SEQ ID NO: 73), 191 amino acids (SEQID NO: 74), 171 amino acids (SEQ ID NO: 75), 172 amino acids (SEQ ID NO:77 or 78), 170 amino acids (SEQ ID NO: 80 or 81), 281 amino acids (SEQID NO: 83 or 84), 289 amino acids (SEQ ID NO: 86 or 87), 177 amino acids(SEQ ID NO: 88), 178 amino acids (SEQ ID NO: 89), 191 amino acids (SEQID NO: 98 or 99), 317 amino acids (SEQ ID NO: 101 or 102), 284 aminoacids (SEQ ID NO: 104 or 105), 437 amino acids (SEQ ID NO: 107 or 108),343 amino acids (SEQ ID NO: 113 or 114), 336 amino acids (SEQ ID NO: 119or 120), 284 amino acids (SEQ ID NO: 122 or 123), 426 amino acids (SEQID NO: 125 or 126), 355 amino acids (SEQ ID NO: 131 or 132), 291 aminoacids (SEQ ID NO: 137 or 138), 286 amino acids (SEQ ID NO: 140 or 141),284 amino acids (SEQ ID NO: 146 or 147), 306 amino acids (SEQ ID NO: 148or 149), 284 amino acids (SEQ ID NO: 149 or 150), 298 amino acids (SEQID NO: 155 or 156), 298 amino acids (SEQ ID NO: 158 or 159), 285 aminoacids (SEQ ID NO: 161 or 162), 340 amino acids (SEQ ID NO: 164 or 165),351 amino acids (SEQ ID NO: 167 or 168), 284 amino acids (SEQ ID NO: 170or 171), 343 amino acids (SEQ ID NO: 173 or 174) or 304 amino acids (SEQID NO: 176 or 177).

In another aspect, a fragment contains at least 96% of the amino acidsof the mature polypeptide, such as 290 amino acids (SEQ ID NO: 8 or 9),291 amino acids (SEQ ID NO: 11 or 12), 367 amino acids (SEQ ID NO: 14 or15), 363 amino acids (SEQ ID NO: 17 or 18), 299 amino acids (SEQ ID NO:20 or 21), 290 amino acids (SEQ ID NO: 23 or 24), 297 amino acids (SEQID NO: 26 or 27), 420 amino acids (SEQ ID NO: 29 or 30), 428 amino acids(SEQ ID NO: 32 or 33), 420 amino acids (SEQ ID NO: 35 or 36), 428 aminoacids (SEQ ID NO: 38 or 39), 305 amino acids (SEQ ID NO: 41 or 42), 313amino acids (SEQ ID NO: 44 or 45), 290 amino acids (SEQ ID NO: 47 or48), 299 amino acids (SEQ ID NO: 50 or 51), 349 amino acids (SEQ ID NO:53 or 54), 358 amino acids (SEQ ID NO: 56 or 57), 419 amino acids (SEQID NO: 59 or 60), 426 amino acids (SEQ ID NO: 62 or 63), 290 amino acids(SEQ ID NO: 65 or 66), 299 amino acids (SEQ ID NO: 68 or 69), 369 aminoacids (SEQ ID NO: 70), 276 amino acids (SEQ ID NO: 71), 296 amino acids(SEQ ID NO: 72), 187 amino acids (SEQ ID NO: 73), 195 amino acids (SEQID NO: 74), 175 amino acids (SEQ ID NO: 75), 176 amino acids (SEQ ID NO:77 or 78), 174 amino acids (SEQ ID NO: 80 or 81), 287 amino acids (SEQID NO: 83 or 84), 295 amino acids (SEQ ID NO: 86 or 87), 180 amino acids(SEQ ID NO: 88), 181 amino acids (SEQ ID NO: 89), 195 amino acids (SEQID NO: 98 or 99), 324 amino acids (SEQ ID NO: 101 or 102), 290 aminoacids (SEQ ID NO: 104 or 105), 446 amino acids (SEQ ID NO: 107 or 108),350 amino acids (SEQ ID NO: 113 or 114), 343 amino acids (SEQ ID NO: 119or 120), 290 amino acids (SEQ ID NO: 122 or 123), 435 amino acids (SEQID NO: 125 or 126), 362 amino acids (SEQ ID NO: 131 or 132), 297 aminoacids (SEQ ID NO: 137 or 138), 292 amino acids (SEQ ID NO: 140 or 141),290 amino acids (SEQ ID NO: 146 or 147), 312 amino acids (SEQ ID NO: 148or 149), 290 amino acids (SEQ ID NO: 149 or 150), 304 amino acids (SEQID NO: 155 or 156), 304 amino acids (SEQ ID NO: 158 or 159), 291 aminoacids (SEQ ID NO: 161 or 162), 347 amino acids (SEQ ID NO: 164 or 165),359 amino acids (SEQ ID NO: 167 or 168), 290 amino acids (SEQ ID NO: 170or 171), 350 amino acids (SEQ ID NO: 173 or 174) or 311 amino acids (SEQID NO: 176 or 177).

In another aspect, a fragment contains at least 98% of the amino acidsof the mature polypeptide, such as 296 amino acids (SEQ ID NO: 8 or 9),297 amino acids (SEQ ID NO: 11 or 12), 374 amino acids (SEQ ID NO: 14 or15), 370 amino acids (SEQ ID NO: 17 or 18), 305 amino acids (SEQ ID NO:20 or 21), 296 amino acids (SEQ ID NO: 23 or 24), 303 amino acids (SEQID NO: 26 or 27), 429 amino acids (SEQ ID NO: 29 or 30), 437 amino acids(SEQ ID NO: 32 or 33), 429 amino acids (SEQ ID NO: 35 or 36), 437 aminoacids (SEQ ID NO: 38 or 39), 312 amino acids (SEQ ID NO: 41 or 42), 319amino acids (SEQ ID NO: 44 or 45), 296 amino acids (SEQ ID NO: 47 or48), 305 amino acids (SEQ ID NO: 50 or 51), 357 amino acids (SEQ ID NO:53 or 54), 366 amino acids (SEQ ID NO: 56 or 57), 427 amino acids (SEQID NO: 59 or 60), 435 amino acids (SEQ ID NO: 62 or 63), 296 amino acids(SEQ ID NO: 65 or 66), 305 amino acids (SEQ ID NO: 68 or 69), 376 aminoacids (SEQ ID NO: 70), 282 amino acids (SEQ ID NO: 71), 302 amino acids(SEQ ID NO: 72), 191 amino acids (SEQ ID NO: 73), 199 amino acids (SEQID NO: 74), 178 amino acids (SEQ ID NO: 75), 179 amino acids (SEQ ID NO:77 or 78), 177 amino acids (SEQ ID NO: 80 or 81), 293 amino acids (SEQID NO: 83 or 84), 301 amino acids (SEQ ID NO: 86 or 87), 184 amino acids(SEQ ID NO: 88), 185 amino acids (SEQ ID NO: 89), 199 amino acids (SEQID NO: 98 or 99), 331 amino acids (SEQ ID NO: 101 or 102), 296 aminoacids (SEQ ID NO: 104 or 105), 455 amino acids (SEQ ID NO: 107 or 108),357 amino acids (SEQ ID NO: 113 or 114), 350 amino acids (SEQ ID NO: 119or 120), 296 amino acids (SEQ ID NO: 122 or 123), 444 amino acids (SEQID NO: 125 or 126), 370 amino acids (SEQ ID NO: 131 or 132), 303 aminoacids (SEQ ID NO: 137 or 138), 298 amino acids (SEQ ID NO: 140 or 141),296 amino acids (SEQ ID NO: 146 or 147), 319 amino acids (SEQ ID NO: 148or 149), 296 amino acids (SEQ ID NO: 149 or 150), 310 amino acids (SEQID NO: 155 or 156), 310 amino acids (SEQ ID NO: 158 or 159), 297 aminoacids (SEQ ID NO: 161 or 162), 354 amino acids (SEQ ID NO: 164 or 165),366 amino acids (SEQ ID NO: 167 or 168), 296 amino acids (SEQ ID NO: 170or 171), 357 amino acids (SEQ ID NO: 173 or 174) or 317 amino acids (SEQID NO: 176 or 177).

In another aspect, a fragment contains at least 99% of the amino acidsof the mature polypeptide, such as 299 amino acids (SEQ ID NO: 8 or 9),300 amino acids (SEQ ID NO: 11 or 12), 378 amino acids (SEQ ID NO: 14 or15), 374 amino acids (SEQ ID NO: 17 or 18), 308 amino acids (SEQ ID NO:20 or 21), 299 amino acids (SEQ ID NO: 23 or 24), 306 amino acids (SEQID NO: 26 or 27), 434 amino acids (SEQ ID NO: 29 or 30), 442 amino acids(SEQ ID NO: 32 or 33), 434 amino acids (SEQ ID NO: 35 or 36), 442 aminoacids (SEQ ID NO: 38 or 39), 315 amino acids (SEQ ID NO: 41 or 42), 323amino acids (SEQ ID NO: 44 or 45), 299 amino acids (SEQ ID NO: 47 or48), 308 amino acids (SEQ ID NO: 50 or 51), 360 amino acids (SEQ ID NO:53 or 54), 369 amino acids (SEQ ID NO: 56 or 57), 432 amino acids (SEQID NO: 59 or 60), 440 amino acids (SEQ ID NO: 62 or 63), 299 amino acids(SEQ ID NO: 65 or 66), 308 amino acids (SEQ ID NO: 68 or 69), 380 aminoacids (SEQ ID NO: 70), 285 amino acids (SEQ ID NO: 71), 305 amino acids(SEQ ID NO: 72), 193 amino acids (SEQ ID NO: 73), 201 amino acids (SEQID NO: 74), 180 amino acids (SEQ ID NO: 75), 181 amino acids (SEQ ID NO:77 or 78), 179 amino acids (SEQ ID NO: 80 or 81), 296 amino acids (SEQID NO: 83 or 84), 304 amino acids (SEQ ID NO: 86 or 87), 186 amino acids(SEQ ID NO: 88), 187 amino acids (SEQ ID NO: 89), 201 amino acids (SEQID NO: 98 or 99), 334 amino acids (SEQ ID NO: 101 or 102), 299 aminoacids (SEQ ID NO: 104 or 105), 460 amino acids (SEQ ID NO: 107 or 108),361 amino acids (SEQ ID NO: 113 or 114), 354 amino acids (SEQ ID NO: 119or 120), 299 amino acids (SEQ ID NO: 122 or 123), 449 amino acids (SEQID NO: 125 or 126), 374 amino acids (SEQ ID NO: 131 or 132), 306 aminoacids (SEQ ID NO: 137 or 138), 301 amino acids (SEQ ID NO: 140 or 141),299 amino acids (SEQ ID NO: 146 or 147), 322 amino acids (SEQ ID NO: 148or 149), 299 amino acids (SEQ ID NO: 149 or 150), 313 amino acids (SEQID NO: 155 or 156), 313 amino acids (SEQ ID NO: 158 or 159), 300 aminoacids (SEQ ID NO: 161 or 162), 358 amino acids (SEQ ID NO: 164 or 165),370 amino acids (SEQ ID NO: 167 or 168), 299 amino acids (SEQ ID NO: 170or 171), 361 amino acids (SEQ ID NO: 173 or 174) or 320 amino acids (SEQID NO: 176 or 177).

Highly branched xylan: The term “highly branched xylan” means that morethan 50% of xylosyl units in the arabinoxylan backbone are substituted.This is preferably calculated from linkage analysis as performed inHuismann et al. Carbohydrate Polymers, 2000, 42:269-279.

Host cell: The term “host cell” means any cell type that is susceptibleto transformation, transfection, transduction, or the like with anucleic acid construct or expression vector comprising a polynucleotideof the present invention. The term “host cell” encompasses any progenyof a parent cell that is not identical to the parent cell due tomutations that occur during replication.

Isolated: The term “isolated” means a substance in a form or environmentthat does not occur in nature. Non-limiting examples of isolatedsubstances include (1) any non-naturally occurring substance, (2) anysubstance including, but not limited to, any enzyme, variant, nucleicacid, protein, peptide or cofactor, that is at least partially removedfrom one or more or all of the naturally occurring constituents withwhich it is associated in nature; (3) any substance modified by the handof man relative to that substance found in nature; or (4) any substancemodified by increasing the amount of the substance relative to othercomponents with which it is naturally associated (e.g., recombinantproduction in a host cell; multiple copies of a gene encoding thesubstance; and use of a stronger promoter than the promoter naturallyassociated with the gene encoding the substance).

Mature polypeptide: The term “mature polypeptide” means a polypeptide inits final form following translation and any post-translationalmodifications, such as N-terminal processing, C-terminal truncation,glycosylation, phosphorylation, etc.

In one aspect, the mature polypeptide is amino acids 1 to 302 of SEQ IDNO: 8 and amino acids −26 to −1 of SEQ ID NO: 2 are a signal peptide. Inanother aspect, the mature polypeptide is amino acids 1 to 302 of SEQ IDNO: 9.

In one aspect, the mature polypeptide is amino acids 1 to 303 of SEQ IDNO: 11 and amino acids −26 to −1 of SEQ ID NO: 11 are a signal peptide.In another aspect, the mature polypeptide is amino acids 1 to 303 of SEQID NO: 12.

In one aspect, the mature polypeptide is amino acids 1 to 382 of SEQ IDNO: 14 and amino acids −21 to −1 of SEQ ID NO: 15 are a signal peptide.In another aspect, the mature polypeptide is amino acids 1 to 382 of SEQID NO: 15.

In one aspect, the mature polypeptide is amino acids 1 to 378 of SEQ IDNO: 17 and amino acids −17 to −1 of SEQ ID NO: 17 are a signal peptide.In another aspect, the mature polypeptide is amino acids 1 to 378 of SEQID NO: 18.

In one aspect, the mature polypeptide is amino acids 1 to 311 of SEQ IDNO: 20 and amino acids −20 to −1 of SEQ ID NO: 20 are a signal peptide.In another aspect, the mature polypeptide is amino acids 1 to 311 of SEQID NO: 21.

In one aspect, the mature polypeptide is amino acids 1 to 302 of SEQ IDNO: 23 and amino acids −29 to −1 of SEQ ID NO: 23 are a signal peptide.In another aspect, the mature polypeptide is amino acids 1 to 302 of SEQID NO: 24.

In one aspect, the mature polypeptide is amino acids 1 to 309 of SEQ IDNO: 26 and amino acids −16 to −1 of SEQ ID NO: 26 are a signal peptide.In another aspect, the mature polypeptide is amino acids 1 to 309 of SEQID NO: 27.

In one aspect, the mature polypeptide is amino acids 1 to 438 of SEQ IDNO: 29 and amino acids −36 to −1 of SEQ ID NO: 29 are a signal peptide.In another aspect, the mature polypeptide is amino acids 1 to 438 of SEQID NO: 30. In one aspect, the mature polypeptide is amino acids 1 to 446of SEQ ID NO: 32 and amino acids −27 to −1 of SEQ ID NO: 32 are a signalpeptide. In another aspect, the mature polypeptide is amino acids 1 to446 of SEQ ID NO: 33.

In one aspect, the mature polypeptide is amino acids 1 to 438 of SEQ IDNO: 35 and amino acids −36 to −1 of SEQ ID NO: 35 are a signal peptide.In another aspect, the mature polypeptide is amino acids 1 to 438 of SEQID NO: 36. In one aspect, the mature polypeptide is amino acids 1 to 446of SEQ ID NO: 38 and amino acids −27 to −1 of SEQ ID NO: 38 are a signalpeptide. In another aspect, the mature polypeptide is amino acids 1 to446 of SEQ ID NO: 39.

In one aspect, the mature polypeptide is amino acids 1 to 318 of SEQ IDNO: 41 and amino acids −18 to −1 of SEQ ID NO: 41 are a signal peptide.In another aspect, the mature polypeptide is amino acids 1 to 318 of SEQID NO: 42. In one aspect, the mature polypeptide is amino acids 1 to 326of SEQ ID NO: 44 and amino acids −18 to −1 of SEQ ID NO: 44 are a signalpeptide. In another aspect, the mature polypeptide is amino acids 1 to326 of SEQ ID NO: 45.

In one aspect, the mature polypeptide is amino acids 1 to 302 of SEQ IDNO: 47 and amino acids −25 to −1 of SEQ ID NO: 47 are a signal peptide.In another aspect, the mature polypeptide is amino acids 1 to 302 of SEQID NO: 48. In one aspect, the mature polypeptide is amino acids 1 to 311of SEQ ID NO: 50 and amino acids −25 to −1 of SEQ ID NO: 50 are a signalpeptide. In another aspect, the mature polypeptide is amino acids 1 to311 of SEQ ID NO: 51.

In one aspect, the mature polypeptide is amino acids 1 to 364 of SEQ IDNO: 53 and amino acids −24 to −1 of SEQ ID NO: 53 are a signal peptide.In another aspect, the mature polypeptide is amino acids 1 to 364 of SEQID NO: 54. In one aspect, the mature polypeptide is amino acids 1 to 373of SEQ ID NO: 56 and amino acids −24 to −1 of SEQ ID NO: 56 are a signalpeptide. In another aspect, the mature polypeptide is amino acids 1 to373 of SEQ ID NO: 57.

In one aspect, the mature polypeptide is amino acids 1 to 436 of SEQ IDNO: 59 and amino acids −31 to −1 of SEQ ID NO: 59 are a signal peptide.In another aspect, the mature polypeptide is amino acids 1 to 436 of SEQID NO: 60. In one aspect, the mature polypeptide is amino acids 1 to 444of SEQ ID NO: 62 and amino acids −27 to −1 of SEQ ID NO: 62 are a signalpeptide. In another aspect, the mature polypeptide is amino acids 1 to444 of SEQ ID NO: 63.

In one aspect, the mature polypeptide is amino acids 1 to 302 of SEQ IDNO: 65 and amino acids −19 to −1 of SEQ ID NO: 65 are a signal peptide.In another aspect, the mature polypeptide is amino acids 1 to 302 of SEQID NO: 66. In one aspect, the mature polypeptide is amino acids 1 to 311of SEQ ID NO: 68 and amino acids −19 to −1 of SEQ ID NO: 68 are a signalpeptide. In another aspect, the mature polypeptide is amino acids 1 to311 of SEQ ID NO: 69.

In one aspect, the mature polypeptide is amino acids 1 to 183 of SEQ IDNO: 77 and amino acids −27 to −1 of SEQ ID NO: 77 are a signal peptide.In another aspect, the mature polypeptide is amino acids 1 to 302 of SEQID NO: 78. In one aspect, the mature polypeptide is amino acids 1 to 181of SEQ ID NO: 80 and amino acids −27 to −1 of SEQ ID NO: 80 are a signalpeptide. In another aspect, the mature polypeptide is amino acids 1 to181 of SEQ ID NO: 81.

In one aspect, the mature polypeptide is amino acids 1 to 299 of SEQ IDNO: 83 and amino acids −42 to −1 of SEQ ID NO: 83 are a signal peptide.In another aspect, the mature polypeptide is amino acids 1 to 299 of SEQID NO: 84. In one aspect, the mature polypeptide is amino acids 1 to 307of SEQ ID NO: 86 and amino acids −27 to −1 of SEQ ID NO: 86 are a signalpeptide. In another aspect, the mature polypeptide is amino acids 1 to307 of SEQ ID NO: 87.

In one aspect, the mature polypeptide is amino acids 1 to 203 of SEQ IDNO: 98 and amino acids −19 to −1 of SEQ ID NO: 98 are a signal peptide.In another aspect, the mature polypeptide is amino acids 1 to 203 of SEQID NO: 99.

In one aspect, the mature polypeptide is amino acids 1 to 337 of SEQ IDNO: 101 and amino acids −18 to −1 of SEQ ID NO: 101 are a signalpeptide. In another aspect, the mature polypeptide is amino acids 1 to337 of SEQ ID NO: 102.

In one aspect, the mature polypeptide is amino acids 1 to 302 of SEQ IDNO: 104 and amino acids −24 to −1 of SEQ ID NO: 104 are a signalpeptide. In another aspect, the mature polypeptide is amino acids 1 to302 of SEQ ID NO: 105.

In one aspect, the mature polypeptide is amino acids 1 to 464 of SEQ IDNO: 107 and amino acids −36 to −1 of SEQ ID NO: 107 are a signalpeptide. In another aspect, the mature polypeptide is amino acids 1 to464 of SEQ ID NO: 108. In one aspect, the mature polypeptide is aminoacids 1 to 472 of SEQ ID NO: 110 and amino acids −27 to −1 of SEQ ID NO:110 are a signal peptide. In another aspect, the mature polypeptide isamino acids 1 to 472 of SEQ ID NO: 111.

In one aspect, the mature polypeptide is amino acids 1 to 364 of SEQ IDNO: 113 and amino acids −18 to −1 of SEQ ID NO: 113 are a signalpeptide. In another aspect, the mature polypeptide is amino acids 1 to364 of SEQ ID NO: 114. In one aspect, the mature polypeptide is aminoacids 1 to 372 of SEQ ID NO: 116 and amino acids −18 to −1 of SEQ ID NO:116 are a signal peptide. In another aspect, the mature polypeptide isamino acids 1 to 372 of SEQ ID NO: 117.

In one aspect, the mature polypeptide is amino acids 1 to 357 of SEQ IDNO: 119 and amino acids −27 to −1 of SEQ ID NO: 119 are a signalpeptide. In another aspect, the mature polypeptide is amino acids 1 to357 of SEQ ID NO: 120.

In one aspect, the mature polypeptide is amino acids 1 to 302 of SEQ IDNO: 122 and amino acids −24 to −1 of SEQ ID NO: 122 are a signalpeptide. In another aspect, the mature polypeptide is amino acids 1 to302 of SEQ ID NO: 123.

In one aspect, the mature polypeptide is amino acids 1 to 453 of SEQ IDNO: 125 and amino acids −39 to −1 of SEQ ID NO: 125 are a signalpeptide. In another aspect, the mature polypeptide is amino acids 1 to453 of SEQ ID NO: 126. In one aspect, the mature polypeptide is aminoacids 1 to 461 of SEQ ID NO: 128 and amino acids −27 to −1 of SEQ ID NO:128 are a signal peptide. In another aspect, the mature polypeptide isamino acids 1 to 461 of SEQ ID NO: 129.

In one aspect, the mature polypeptide is amino acids 1 to 377 of SEQ IDNO: 131 and amino acids −20 to −1 of SEQ ID NO: 131 are a signalpeptide. In another aspect, the mature polypeptide is amino acids 1 to377 of SEQ ID NO: 132. In one aspect, the mature polypeptide is aminoacids 1 to 385 of SEQ ID NO: 134 and amino acids −20 to −1 of SEQ ID NO:134 are a signal peptide. In another aspect, the mature polypeptide isamino acids 1 to 385 of SEQ ID NO: 135.

In one aspect, the mature polypeptide is amino acids 1 to 309 of SEQ IDNO: 137 and amino acids −26 to −1 of SEQ ID NO: 137 are a signalpeptide. In another aspect, the mature polypeptide is amino acids 1 to309 of SEQ ID NO: 138.

In one aspect, the mature polypeptide is amino acids 1 to 304 of SEQ IDNO: 140 and amino acids −21 to −1 of SEQ ID NO: 140 are a signalpeptide. In another aspect, the mature polypeptide is amino acids 1 to304 of SEQ ID NO: 141. In one aspect, the mature polypeptide is aminoacids 1 to 312 of SEQ ID NO: 143 and amino acids −21 to −1 of SEQ ID NO:143 are a signal peptide. In another aspect, the mature polypeptide isamino acids 1 to 312 of SEQ ID NO: 144.

In one aspect, the mature polypeptide is amino acids 1 to 302 of SEQ IDNO: 146 and amino acids −26 to −1 of SEQ ID NO: 146 are a signalpeptide. In another aspect, the mature polypeptide is amino acids 1 to302 of SEQ ID NO: 147.

In one aspect, the mature polypeptide is amino acids 1 to 302 of SEQ IDNO: 149 and amino acids −23 to −1 of SEQ ID NO: 149 are a signalpeptide. In another aspect, the mature polypeptide is amino acids 1 to302 of SEQ ID NO: 150. In one aspect, the mature polypeptide is aminoacids 1 to 310 of SEQ ID NO: 152 and amino acids −23 to −1 of SEQ ID NO:152 are a signal peptide. In another aspect, the mature polypeptide isamino acids 1 to 310 of SEQ ID NO: 153.

In one aspect, the mature polypeptide is amino acids 1 to 316 of SEQ IDNO: 155 and amino acids −26 to −1 of SEQ ID NO: 155 are a signalpeptide. In another aspect, the mature polypeptide is amino acids 1 to316 of SEQ ID NO: 156.

In one aspect, the mature polypeptide is amino acids 1 to 316 of SEQ IDNO: 158 and amino acids −15 to −1 of SEQ ID NO: 158 are a signalpeptide. In another aspect, the mature polypeptide is amino acids 1 to316 of SEQ ID NO: 159.

In one aspect, the mature polypeptide is amino acids 1 to 303 of SEQ IDNO: 161 and amino acids −16 to −1 of SEQ ID NO: 161 are a signalpeptide. In another aspect, the mature polypeptide is amino acids 1 to303 of SEQ ID NO: 162.

In one aspect, the mature polypeptide is amino acids 1 to 361 of SEQ IDNO: 164 and amino acids −27 to −1 of SEQ ID NO: 164 are a signalpeptide. In another aspect, the mature polypeptide is amino acids 1 to361 of SEQ ID NO: 165.

In one aspect, the mature polypeptide is amino acids 1 to 373 of SEQ IDNO: 167 and amino acids −24 to −1 of SEQ ID NO: 167 are a signalpeptide. In another aspect, the mature polypeptide is amino acids 1 to373 of SEQ ID NO: 168.

In one aspect, the mature polypeptide is amino acids 1 to 302 of SEQ IDNO: 170 and amino acids −22 to −1 of SEQ ID NO: 170 are a signalpeptide. In another aspect, the mature polypeptide is amino acids 1 to302 of SEQ ID NO: 171.

In one aspect, the mature polypeptide is amino acids 1 to 364 of SEQ IDNO: 173 and amino acids −19 to −1 of SEQ ID NO: 173 are a signalpeptide. In another aspect, the mature polypeptide is amino acids 1 to364 of SEQ ID NO: 174.

In one aspect, the mature polypeptide is amino acids 1 to 323 of SEQ IDNO: 176 and amino acids −21 to −1 of SEQ ID NO: 176 are a signalpeptide. In another aspect, the mature polypeptide is amino acids 1 to323 of SEQ ID NO: 177. In one aspect, the mature polypeptide is aminoacids 1 to 331 of SEQ ID NO: 179 and amino acids −21 to −1 of SEQ ID NO:179 are a signal peptide. In another aspect, the mature polypeptide isamino acids 1 to 331 of SEQ ID NO: 180.

It is known in the art that a host cell may produce a mixture of two ofmore different mature polypeptides (i.e., with a different C-terminaland/or N-terminal amino acid) expressed by the same polynucleotide. Itis also known in the art that different host cells process polypeptidesdifferently, and thus, one host cell expressing a polynucleotide mayproduce a different mature polypeptide (e.g., having a differentC-terminal and/or N-terminal amino acid) as compared to another hostcell expressing the same polynucleotide.

Mature polypeptide coding sequence: The term “mature polypeptide codingsequence” means a polynucleotide that encodes a mature polypeptidehaving arabinofuranosidase or xylanase activity. In one aspect, themature polypeptide coding sequence is nucleotides 79 to 987 of SEQ IDNO: 10; nucleotides 1 to 78 of SEQ ID NO: 10 encode a signal peptide.

In one aspect, the mature polypeptide coding sequence is the joinedsequence of nucleotides 49 to 70 and nucleotides 123 to 1027 of SEQ IDNO: 25 or the cDNA sequence thereof; nucleotides 1 to 48 of SEQ ID NO:25 encode a signal peptide.

In one aspect, the mature polypeptide coding sequence is nucleotides 88to 993 of SEQ ID NO: 22; nucleotides 1 to 87 of SEQ ID NO: 22 encode asignal peptide.

In one aspect, the mature polypeptide coding sequence is nucleotides 109to 1422 of SEQ ID NO: 28; nucleotides 1 to 108 of SEQ ID NO: 28 encode asignal peptide.

In one aspect, the mature polypeptide coding sequence is nucleotides 82to 1419 of SEQ ID NO: 31; nucleotides 1 to 81 of SEQ ID NO: 31 encode asignal peptide.

In one aspect, the mature polypeptide coding sequence is nucleotides 109to 1422 of SEQ ID NO: 34; nucleotides 1 to 108 of SEQ ID NO: 34 encode asignal peptide.

In one aspect, the mature polypeptide coding sequence is nucleotides 82to 1419 of SEQ ID NO: 37; nucleotides 1 to 81 of SEQ ID NO: 37 encode asignal peptide.

In one aspect, the mature polypeptide coding sequence is nucleotides 76to 981 of SEQ ID NO: 46; nucleotides 1 to 75 of SEQ ID NO: 46 encode asignal peptide.

In one aspect, the mature polypeptide coding sequence is nucleotides 76to 1008 of SEQ ID NO: 49; nucleotides 1 to 75 of SEQ ID NO: 49 encode asignal peptide.

In one aspect, the mature polypeptide coding sequence is the joinedsequence of nucleotides 73 to 318, nucleotides 470 to 1298 andnucleotides 1392 to 1408 of SEQ ID NO: 52; nucleotides 1 to 72 of SEQ IDNO: 52 encode a signal peptide.

In one aspect, the mature polypeptide coding sequence is the joinedsequence of nucleotides 73 to 318, nucleotides 470 to 1298 andnucleotides 1392 to 1435 of SEQ ID NO: 55; nucleotides 1 to 72 of SEQ IDNO: 55 encode a signal peptide.

In one aspect, the mature polypeptide coding sequence is nucleotides 94to 1401 of SEQ ID NO: 58; nucleotides 1 to 93 of SEQ ID NO: 58 encode asignal peptide.

In one aspect, the mature polypeptide coding sequence is nucleotides 82to 1413 of SEQ ID NO: 61; nucleotides 1 to 81 of SEQ ID NO: 61 encode asignal peptide.

In one aspect, the mature polypeptide coding sequence is the joinedsequence of nucleotides 58 to 330, nucleotides 403 to 655, nucleotides795 to 948 and nucleotides 1100 to 1325 of SEQ ID NO: 64; nucleotides 1to 57 of SEQ ID NO: 64 encode a signal peptide.

In one aspect, the mature polypeptide coding sequence is the joinedsequence of nucleotides 58 to 330, nucleotides 403 to 655, nucleotides795 to 948 and nucleotides 1100 to 1352 of SEQ ID NO: 67; nucleotides 1to 57 of SEQ ID NO: 67 encode a signal peptide.

In one aspect, the mature polypeptide coding sequence is nucleotides 82to 633 of SEQ ID NO: 76; nucleotides 1 to 81 of SEQ ID NO: 76 encode asignal peptide.

In one aspect, the mature polypeptide coding sequence is nucleotides 82to 624 of SEQ ID NO: 79; nucleotides 1 to 81 of SEQ ID NO: 79 encode asignal peptide.

In one aspect, the mature polypeptide coding sequence is nucleotides 127to 1023 of SEQ ID NO: 82; nucleotides 1 to 126 of SEQ ID NO: 82 encode asignal peptide.

In one aspect, the mature polypeptide coding sequence is nucleotides 82to 1002 of SEQ ID NO: 85; nucleotides 1 to 81 of SEQ ID NO: 85 encode asignal peptide.

In one aspect, the mature polypeptide coding sequence is the joinedsequence of nucleotides 58 to 269 and nucleotides 328 to 724 of SEQ IDNO: 97; nucleotides 1 to 57 of SEQ ID NO: 97 encode a signal peptide.

In one aspect, the mature polypeptide coding sequence is the joinedsequence of nucleotides 55 to 71, nucleotides 121 to 524, nucleotides594 to 1054 and nucleotides 1142 to 1270 of SEQ ID NO: 100; nucleotides1 to 54 of SEQ ID NO: 100 encode a signal peptide.

In one aspect, the mature polypeptide coding sequence is nucleotides 73to 978 of SEQ ID NO: 103; nucleotides 1 to 72 of SEQ ID NO: 103 encode asignal peptide.

In one aspect, the mature polypeptide coding sequence is nucleotides 109to 1500 of SEQ ID NO: 106; nucleotides 1 to 108 of SEQ ID NO: 106 encodea signal peptide.

In one aspect, the mature polypeptide coding sequence is nucleotides 82to 1497 of SEQ ID NO: 109; nucleotides 1 to 81 of SEQ ID NO: 109 encodea signal peptide.

In one aspect, the mature polypeptide coding sequence is nucleotides 55to 1146 of SEQ ID NO: 112; nucleotides 1 to 54 of SEQ ID NO: 112 encodea signal peptide.

In one aspect, the mature polypeptide coding sequence is nucleotides 55to 1170 of SEQ ID NO: 115; nucleotides 1 to 54 of SEQ ID NO: 115 encodea signal peptide.

In one aspect, the mature polypeptide coding sequence is the joinedsequence of nucleotides 82 to 1135 and nucleotides 1226 to 1242 of SEQID NO: 118; nucleotides 1 to 81 of SEQ ID NO: 118 encode a signalpeptide.

In one aspect, the mature polypeptide coding sequence is nucleotides 73to 978 of SEQ ID NO: 121; nucleotides 1 to 72 of SEQ ID NO: 121 encode asignal peptide.

In one aspect, the mature polypeptide coding sequence is nucleotides 118to 1476 of SEQ ID NO: 124; nucleotides 1 to 117 of SEQ ID NO: 124 encodea signal peptide.

In one aspect, the mature polypeptide coding sequence is nucleotides 82to 1464 of SEQ ID NO: 127; nucleotides 1 to 81 of SEQ ID NO: 127 encodea signal peptide.

In one aspect, the mature polypeptide coding sequence is the joinedsequence of nucleotides 61 to 93, nucleotides 152 to 162, nucleotides216 to 262 and nucleotides 323 to 1362 of SEQ ID NO: 130; nucleotides 1to 60 of SEQ ID NO: 130 encode a signal peptide.

In one aspect, the mature polypeptide coding sequence is the joinedsequence of nucleotides 61 to 93, nucleotides 152 to 162, nucleotides216 to 262 and nucleotides 323 to 1386 of SEQ ID NO: 133; nucleotides 1to 60 of SEQ ID NO: 133 encode a signal peptide.

In one aspect, the mature polypeptide coding sequence is nucleotides 79to 1005 of SEQ ID NO: 136; nucleotides 1 to 78 of SEQ ID NO: 136 encodea signal peptide.

In one aspect, the mature polypeptide coding sequence is the joinedsequence of nucleotides 64 to 358 and nucleotides 512 to 1128 of SEQ IDNO: 139; nucleotides 1 to 63 of SEQ ID NO: 139 encode a signal peptide.

In one aspect, the mature polypeptide coding sequence is the joinedsequence of nucleotides 64 to 358 and nucleotides 512 to 1152 of SEQ IDNO: 142; nucleotides 1 to 63 of SEQ ID NO: 142 encode a signal peptide.

In one aspect, the mature polypeptide coding sequence is nucleotides 79to 984 of SEQ ID NO: 145; nucleotides 1 to 78 of SEQ ID NO: 145 encode asignal peptide.

In one aspect, the mature polypeptide coding sequence is nucleotides 70to 975 of SEQ ID NO: 148; nucleotides 1 to 69 of SEQ ID NO: 148 encode asignal peptide.

In one aspect, the mature polypeptide coding sequence is nucleotides 70to 999 of SEQ ID NO: 151; nucleotides 1 to 69 of SEQ ID NO: 151 encode asignal peptide.

In one aspect, the mature polypeptide coding sequence is nucleotides 79to 1026 of SEQ ID NO: 154; nucleotides 1 to 78 of SEQ ID NO: 154 encodea signal peptide.

In one aspect, the mature polypeptide coding sequence is nucleotides 46to 993 of SEQ ID NO: 157; nucleotides 1 to 45 of SEQ ID NO: 157 encode asignal peptide.

In one aspect, the mature polypeptide coding sequence is nucleotides 49to 957 of SEQ ID NO: 160; nucleotides 1 to 48 of SEQ ID NO: 160 encode asignal peptide.

In one aspect, the mature polypeptide coding sequence is the joinedsequence of nucleotides 82 to 1147 and nucleotides 1208 to 1224 of SEQID NO: 163; nucleotides 1 to 81 of SEQ ID NO: 163 encode a signalpeptide.

In one aspect, the mature polypeptide coding sequence is the joinedsequence of nucleotides 73 to 318, nucleotides 478 to 1333 andnucleotides 1396 to 1412 of SEQ ID NO: 166; nucleotides 1 to 72 of SEQID NO: 166 encode a signal peptide.

In one aspect, the mature polypeptide coding sequence is the joinedsequence of nucleotides 67 to 95, nucleotides 229 to 469, nucleotides435 to 940 and nucleotides 1052 to 1280 of SEQ ID NO: 169; nucleotides 1to 66 of SEQ ID NO: 169 encode a signal peptide.

In one aspect, the mature polypeptide coding sequence is the joinedsequence of nucleotides 58 to 1132 and nucleotides 1199 to 1215 of SEQID NO: 172; nucleotides 1 to 57 of SEQ ID NO: 172 encode a signalpeptide.

In one aspect, the mature polypeptide coding sequence is the joinedsequence of nucleotides 64 to 492, nucleotides 571 to 988 andnucleotides 1080 to 1201 of SEQ ID NO: 175; nucleotides 1 to 63 of SEQID NO: 175 encode a signal peptide.

In one aspect, the mature polypeptide coding sequence is the joinedsequence of nucleotides 64 to 492, nucleotides 571 to 988 andnucleotides 1080 to 1225 of SEQ ID NO: 178; nucleotides 1 to 63 of SEQID NO: 178 encode a signal peptide.

Nucleic acid construct: The term “nucleic acid construct” means anucleic acid molecule, either single- or double-stranded, which isisolated from a naturally occurring gene or is modified to containsegments of nucleic acids in a manner that would not otherwise exist innature or which is synthetic, which comprises one or more controlsequences.

Nutrient Digestibility: The term “nutrient digestibility” means thefraction of a nutrient that disappears from the gastro-intestinal tractor a specified segment of the gastro-intestinal tract, e.g. the smallintestine. Nutrient digestibility may be measured as the differencebetween what is administered to the subject and what. comes out in thefaeces of the subject, or between what is administered to the subjectand what remains in the digesta on a specified segment of the gastrointestinal tract, e.g. the ileum.

Nutrient digestibility as used herein may be measured by the differencebetween the intake of a nutrient and the excreted nutrient by means ofthe total collection of excreta during a period of time; or with the useof an inert marker that is not absorbed by the animal, and allows theresearcher calculating the amount of nutrient that disappeared in theentire gastro-intestinal tract or a segment of the gastro-intestinaltract. Such an inert marker may be titanium dioxide, chromic oxide oracid insoluble ash. Digestibility may be expressed as a percentage ofthe nutrient in the feed, or as mass units of digestible nutrient permass units of nutrient in the feed. Nutrient digestibility as usedherein encompasses starch digestibility, fat digestibility, proteindigestibility, and amino acid digestibility.

Energy digestibility as used herein means the gross energy of the feedconsumed minus the gross energy of the faeces or the gross energy of thefeed consumed minus the gross energy of the remaining digesta on aspecified segment of the gastro-intestinal tract of the animal, e.g. theileum. Metabolizable energy as used herein refers to apparentmetabolizable energy and means the gross energy of the feed consumedminus the gross energy contained in the faeces, urine, and gaseousproducts of digestion. Energy digestibility and metabolizable energy maybe measured as the difference between the intake of gross energy and thegross energy excreted in the faeces or the digesta present in specifiedsegment of the gastro-intestinal tract using the same methods to measurethe digestibility of nutrients, with appropriate corrections fornitrogen excretion to calculate metabolizable energy of feed.

Operably linked: The term “operably linked” means a configuration inwhich a control sequence is placed at an appropriate position relativeto the coding sequence of a polynucleotide such that the controlsequence directs expression of the coding sequence.

Sequence Identity: The relatedness between two amino acid sequences orbetween two nucleotide sequences is described by the parameter “sequenceidentity”.

For purposes of the present invention, the degree of sequence identitybetween two amino acid sequences is determined using theNeedleman-Wunsch algorithm (Needleman and Wunsch, 1970, J. Mol. Biol.48: 443-453) as implemented in the Needle program of the EMBOSS package(EMBOSS: The European Molecular Biology Open Software Suite, Rice etal., 2000, Trends Genet. 16: 276-277), preferably version 3.0.0 orlater. Version 6.1.0 was used. The optional parameters used are gap openpenalty of 10, gap extension penalty of 0.5, and the EBLOSUM62 (EMBOSSversion of BLOSUM62) substitution matrix. The output of Needle labelled“longest identity” (obtained using the—nobrief option) is used as thepercent identity and is calculated as follows:(Identical Residues×100)/(Length of Alignment−Total Number of Gaps inAlignment)

For purposes of the present invention, the degree of sequence identitybetween two deoxyribonucleotide sequences is determined using theNeedleman-Wunsch algorithm (Needleman and Wunsch, 1970, supra) asimplemented in the Needle program of the EMBOSS package (EMBOSS: TheEuropean Molecular Biology Open Software Suite, Rice et al., 2000,supra), preferably version 3.0.0 or later. Version 6.1.0 was used. Theoptional parameters used are gap open penalty of 10, gap extensionpenalty of 0.5, and the EDNAFULL (EMBOSS version of NCBI NUC4.4)substitution matrix. The output of Needle labelled “longest identity”(obtained using the—nobrief option) is used as the percent identity andis calculated as follows:(Identical Deoxyribonucleotides×100)/(Length of Alignment−Total Numberof Gaps in Alignment)

Solubilised xylose from defatted destarched maize (DFDSM): The term“solubilised xylose from defatted destarched maize (DFDSM)” means thetotal amount of xylose measured in the supernatant after incubation withan enzyme compared to the total amount of xylose present in thesubstrate before the incubation with the enzyme. As described herein,the enzyme solubilizes the xylan in the substrate to soluble fragments(polysaccharides). Since the xylose assay only measures xylose (themonosaccharide), the solubilised xylan needs to be hydrolysed by acid inorder to release all of the xylose as monosaccharides before the xyloseassay can be performed. The percentage solubilised xylose from defatteddestarched maize (DFDSM) may be calculated as described in example 23herein and is presented as ‘Percent solubilised xylose’ in the examples.

The term “solubilise at least x % xylose from defatted destarched maize(DFDSM)” means that the total amount of xylose measured in thesupernatant after incubation as described above is at least x % The term“solubilise at least x times more xylose from DFDSM than the GH10 orGH11 polypeptide can when the GH62 polypeptide is not present” meansthat the total amount of xylose measured in the supernatant afterincubation as described above is at least x times higher using thecombination of a GH10 or GH11 xylanase and a GH62 arabinofuranosidasecompared to when the GH10 or GH11 xylanase is used without the GH62arabinofuranosidase being present.

Stringency conditions: The different stringency conditions are definedas follows.

The term “very low stringency conditions” means for probes of at least100 nucleotides in length, prehybridization and hybridization at 42° C.in 5×SSPE, 0.3% SDS, 200 micrograms/ml sheared and denatured salmonsperm DNA, and 25% formamide, following standard Southern blottingprocedures for 12 to 24 hours. The carrier material is finally washedthree times each for 15 minutes using 2.0×SSC, 0.2% SDS at 60° C.

The term “low stringency conditions” means for probes of at least 100nucleotides in length, prehybridization and hybridization at 42° C. in5×SSPE, 0.3% SDS, 200 micrograms/ml sheared and denatured salmon spermDNA, and 25% formamide, following standard Southern blotting proceduresfor 12 to 24 hours. The carrier material is finally washed three timeseach for 15 minutes using 1.0×SSC, 0.2% SDS at 60° C.

The term “medium stringency conditions” means for probes of at least 100nucleotides in length, prehybridization and hybridization at 42° C. in5×SSPE, 0.3% SDS, 200 micrograms/ml sheared and denatured salmon spermDNA, and 35% formamide, following standard Southern blotting proceduresfor 12 to 24 hours. The carrier material is finally washed three timeseach for 15 minutes using 1.0×SSC, 0.2% SDS at 65° C.

The term “medium-high stringency conditions” means for probes of atleast 100 nucleotides in length, prehybridization and hybridization at42° C. in 5×SSPE, 0.3% SDS, 200 micrograms/ml sheared and denaturedsalmon sperm DNA, and 35% formamide, following standard Southernblotting procedures for 12 to 24 hours. The carrier material is finallywashed three times each for 15 minutes using 1.0×SSC, 0.2% SDS at 70° C.

The term “high stringency conditions” means for probes of at least 100nucleotides in length, prehybridization and hybridization at 42° C. in5×SSPE, 0.3% SDS, 200 micrograms/ml sheared and denatured salmon spermDNA, and 50% formamide, following standard Southern blotting proceduresfor 12 to 24 hours. The carrier material is finally washed three timeseach for 15 minutes using 0.5×SSC, 0.2% SDS at 70° C.

The term “very high stringency conditions” means for probes of at least100 nucleotides in length, prehybridization and hybridization at 42° C.in 5×SSPE, 0.3% SDS, 200 micrograms/ml sheared and denatured salmonsperm DNA, and 50% formamide, following standard Southern blottingprocedures for 12 to 24 hours. The carrier material is finally washedthree times each for 15 minutes using 0.5×SSC, 0.2% SDS at 75° C.

Subsequence: The term “subsequence” means a polynucleotide having one ormore (e.g., several) nucleotides absent from the 5′ and/or 3′ end of amature polypeptide coding sequence; wherein the subsequence encodes afragment having arabinofuranosidase or xylanase activity.

Substantially pure polypeptide: The term “substantially purepolypeptide” means a preparation that contains at most 10%, at most 8%,at most 6%, at most 5%, at most 4%, at most 3%, at most 2%, at most 1%,and at most 0.5% by weight of other polypeptide material with which itis natively or recombinantly associated. Preferably, the polypeptide isat least 92% pure, e.g., at least 94% pure, at least 95% pure, at least96% pure, at least 97% pure, at least 98% pure, at least 99%, at least99.5% pure, and 100% pure by weight of the total polypeptide materialpresent in the preparation. The polypeptides of the present inventionare preferably in a substantially pure form. This can be accomplished,for example, by preparing the polypeptide by well-known recombinantmethods or by classical purification methods.

Variant: The term “variant” means a polypeptide having xylanase orarabinofuranosidase activity comprising an alteration, i.e., asubstitution, insertion, and/or deletion of one or more (several) aminoacid residues at one or more (several) positions. A substitution means areplacement of an amino acid occupying a position with a different aminoacid; a deletion means removal of an amino acid occupying a position;and an insertion means adding 1-3 amino acids adjacent to an amino acidoccupying a position.

Xylanase: The term “xylanase” means a 1,4-beta-D-xylan-xylohydrolase(E.C. 3.2.1.8) that catalyses the endohydrolysis of 1,4-beta-D-xylosidiclinkages in xylans. Xylanase activity can be determined with 0.2%AZCL-arabinoxylan as substrate in 0.01% TRITON® X-100 and 200 mM sodiumphosphate pH 6 at 37° C. One unit of xylanase activity is defined as 1.0μmole of azurine produced per minute at 37° C., pH 6 from 0.2%AZCL-arabinoxylan as substrate in 200 mM sodium phosphate pH 6.

Nomenclature

For purposes of the present invention, the nomenclature [Y/F] means thatthe amino acid at this position may be a tyrosine (Try, Y) or aphenylalanine (Phe, F). Likewise the nomenclature [V/G/A/I] means thatthe amino acid at this position may be a valine (Val, V), glycine (Gly,G), alanine (Ala, A) or isoleucine (Ile, I), and so forth for othercombinations as described herein. Unless otherwise limited further, theamino acid X is defined such that it may be any of the 20 natural aminoacids.

DETAILED DESCRIPTION OF THE INVENTION

The inventors have found that certain arabinofuranosidases fromglycoside hydrolase family 62 (herein referred to as GH62) incombination with one or more GH10 or GH11 xylanase are surprisingly goodat solubilising the xylose backbone of sterically hindered arabinoxylanfound in plant based material from the sub-family Panicoideae. This issurprising since arabinofuranosidases which are known to be very good atsolubilising wheat arabinoxylan (e.g. the GH43 from Humicola insolenshaving SEQ ID NO: 1 of WO 2006/114095, the GH51 from Meripilus giganteushaving SEQ ID NO: 2 of WO 2006/114095 or the combination of both) areunable to solubilise the highly substituted arabinoxylan found in e.g.maize, corn, sorghum, switchgrass, millet, pearl millet and foxtailmillet.

The amount of starch present in untreated plant material makes itdifficult to detect significant solubilisation of arabinoxylan. Thusmodel substrates, wherein the starch and fat present in the plantmaterial is removed without effecting the degree of substitution, can beused to aid the determination of improved enzyme combinations over knownprior art combinations. One model substrate is defatted destarched maize(DFDSM) and can be prepared as described in the experimental sectionherein. It is important that the model substrate is not prepared usingstrongly acidic or basic conditions or high temperatures, since suchconditions can remove the side chain carbohydrate molecules and/or estergroups present on the xylan backbone. If these side chain groups areremoved, then the complexity and degree of substitution will be reducedresulting in an arabinoxylan material which is easy to degrade by knownsolutions. It is for this reason that heat, acid and/or basepre-treatment is used in biomass conversion.

The solubilisation of the arabinoxylan can be measured as the amount ofxylose released into the supernatant. Increased amounts ofsolubilisation will result in more xylose being released which can bedetected using e.g. the xylose assay method as described herein. Withoutwishing to be bound by theory, it is believed that increasing thesolubilisation of the arabinoxylan opens up the cell walls that canresult in the nutrients, such as starch, which are trapped inside beingreleased. The release of starch and other nutrients can result inimproved animal performance and/or improved conversion of biomass toe.g. ethanol.

The arabinofuranosidases which have this surprising property allcomprise the motif [H/Y][L/M]F[F/S][A/C/H/S/T/V][A/D/G/N/R]D[D/E/N]G(SEQ ID NO: 1). As far as the inventors are aware, this motif is onlyfound in arabinofuranosidases from family GH62 and are present in thepolypeptides of the invention.

Thus in a first aspect, the invention relates to a compositioncomprising one or more GH10 or GH11 polypeptides having xylanaseactivity and one or more GH62 polypeptides having arabinofuranosidaseactivity, wherein:

-   -   (a) the GH62 polypeptide comprises the motif        [H/Y][L/M]F[F/S][A/C/H/S/T/V][A/D/G/N/R]D[D/E/N]G (SEQ ID NO:        1);    -   (b) the GH10 or GH11 polypeptide and the GH62 polypeptide        together solubilise at least 2.0% xylose from defatted        destarched maize (DFDSM); and    -   (c) the GH10 or GH11 polypeptide and the GH62 polypeptide        together solubilise at least 2 times more xylose from DFDSM than        the GH10 or GH11 polypeptide can when the GH62 polypeptide is        not present;        -   wherein (b) and (c) are performed under the reaction            conditions:            -   i) 25 mg GH10 or GH11 polypeptide per kg DFDSM,            -   ii) 12.5 mg GH62 polypeptide per kg DFDSM, and            -   iii) incubation at 40° C., pH 5 for 4 hours.

In an alternative first aspect, the invention relates to a compositioncomprising one or more GH10 or GH11 polypeptides having xylanaseactivity and one or more GH62 polypeptides having arabinofuranosidaseactivity, wherein:

-   -   (a) the GH62 polypeptide comprises the motif        [H/Y][L/M]F[F/S][A/C/H/S/T/V][A/D/G/N/R]D[D/E/N]G (SEQ ID NO:        1);    -   (b) the GH10 or GH11 polypeptide and the GH62 polypeptide        together solubilise at least 2.0% xylose from defatted        destarched maize (DFDSM); and    -   (c) the GH10 or GH11 polypeptide and the GH62 polypeptide        together solubilise at least 2 times more xylose from DFDSM than        the GH10 or GH11 polypeptide can when the GH62 polypeptide is        not present;        -   wherein (b) and (c) are performed under the reaction            conditions:            -   i) 10 mg GH10 or GH11 polypeptide per kg DFDSM,            -   ii) 10 mg GH62 polypeptide per kg DFDSM, and            -   iii) incubation at 40° C., pH 5 for 4 hours.

In an embodiment, the amino acid in position 1 of the motif is ahistidine or tyrosine. In an embodiment, the amino acid in position 2 ofthe motif is a leucine. In an embodiment, the amino acid in position 4of the motif is a phenylalanine or serine. In an embodiment, the aminoacid in position 5 of the motif is an alanine, serine or valine. In anembodiment, the amino acid in position 6 of the motif is an alanine,aspartic acid or glycine. In an embodiment, the amino acid in position 8of the motif is an asparagine. In a preferred embodiment, the GH62polypeptide comprises the motif [H/Y]LF[F/S][A/S/V][A/D/G]DNG (SEQ IDNO: 2).

In an embodiment, the amino acid in position 1 of the motif is atyrosine. In an embodiment, the amino acid in position 2 of the motif isa leucine. In an embodiment, the amino acid in position 4 of the motifis a phenylalanine. In an embodiment, the amino acid in position 5 ofthe motif is an alanine, cysteine or valine, preferably an alanine orvaline, more preferably an alanine. In an embodiment, the amino acid inposition 6 of the motif is an alanine, aspartic acid or glycine,preferably an alanine or glycine, more preferably a glycine. In anembodiment, the amino acid in position 8 of the motif is an asparagine.In a preferred embodiment, the GH62 polypeptide comprises the motifYLFF[A/V][A/G]DNG (SEQ ID NO: 3), even more preferably the motifYLFFAGDNG (SEQ ID NO: 4).

In an embodiment, the amino acid in position 1 of the motif is ahistidine or tyrosine, preferably a tyrosine. In an embodiment, theamino acid in position 2 of the motif is a leucine. In an embodiment,the amino acid in position 4 of the motif is a serine. In an embodiment,the amino acid in position 5 of the motif is a serine or threonine,preferably a serine. In an embodiment, the amino acid in position 6 ofthe motif is an aspartic acid or glycine, preferably an aspartic acid.In an embodiment, the amino acid in position 8 of the motif is anasparagine. In a preferred embodiment, the GH62 polypeptide comprisesthe motif [H/Y]LFSSDDNG (SEQ ID NO: 5), even more preferably the motifYLFSSDDNG (SEQ ID NO: 6).

In an alternative first aspect, the invention relates to an animal feedor animal feed additive comprising one or more GH10 or GH11 polypeptideshaving xylanase activity and one or more GH62 polypeptides havingarabinofuranosidase activity, wherein:

-   -   (a) the GH62 polypeptide comprises the motif        [H/Y][L/M]F[F/S][A/C/H/S/T/V][A/D/G/N/R]D[D/E/N]G (SEQ ID NO:        1);    -   (b) the GH10 or GH11 polypeptide and the GH62 polypeptide        together solubilise at least 2.0% xylose from defatted        destarched maize (DFDSM);    -   (c) the GH10 or GH11 polypeptide and the GH62 polypeptide        together solubilise at least 2 times more xylose from DFDSM than        the GH10 or GH11 polypeptide can when the GH62 polypeptide is        not present;        -   wherein (b) and (c) are performed under the reaction            conditions:            -   i) 10 mg GH10 or GH11 polypeptide per kg DFDSM,            -   ii) 10 mg GH62 polypeptide per kg DFDSM, and            -   iii) incubation at 40° C., pH 5 for 4 hours;    -   (d) the GH10 or GH11 polypeptide is dosed at 0.01-200 mg enzyme        protein per kg animal feed; and    -   (e) the GH62 polypeptide is dosed at 0.01-200 mg enzyme protein        per kg animal feed.

The following data points were obtained demonstrating the generality ofthe invention.

SEQ SEQ SEQ SEQ SEQ SEQ SEQ SEQ SEQ ID ID ID ID ID ID ID ID ID SEQ IDSEQ ID SEQ ID SEQ ID SEQ ID SEQ ID SEQ ID NO: NO: NO: NO: NO: NO: NO:NO: NO: NO: 70 NO: 71 NO: 72 NO: 73 NO: 74 NO: 75 NO: 78 81 87 88 89 9596 99 102 180 SEQ ID NO: 9 X X X X X X X X X SEQ ID NO: 12 X X X X X XSEQ ID NO: 15 X X SEQ ID NO: 18 X X SEQ ID NO: 21 X X X X SEQ ID NO: 24X X X X X X X X X X X X X X SEQ ID NO: 27 X X X X X X SEQ ID NO: 33 X XX SEQ ID NO: 39 X X SEQ ID NO: 45 X X X SEQ ID NO: 51 X X X X X X X X XX SEQ ID NO: 57 X X X SEQ ID NO: 63 X X SEQ ID NO: 69 X X SEQ ID NO: 111X X X X SEQ ID NO: 117 X X X X SEQ ID NO: 120 X X X X SEQ ID NO: 129 X XX X SEQ ID NO: 135 X X X X SEQ ID NO: 138 X X X X SEQ ID NO: 144 X X X XSEQ ID NO: 147 X X X X SEQ ID NO: 153 X X X X SEQ ID NO: 156 X X X X SEQID NO: 159 X X X X SEQ ID NO: 162 X X X X SEQ ID NO: 165 X X X X SEQ IDNO: 168 X X X X SEQ ID NO: 171 X X X X SEQ ID NO: 174 X X X X SEQ ID NO:105 X X X X SEQ ID NO: 123 X X X XGH62 Polypeptides of the Composition

Preferred embodiments of the first aspect of the invention relating tothe GH62 polypeptide having arabinofuranosidase activity are disclosedherein below.

In an embodiment, the composition comprises a GH62 polypeptide havingarabinofuranosidase activity, wherein GH62 polypeptide havingarabinofuranosidase activity has a sequence identity to the maturepolypeptide of SEQ ID NO: 8 of at least 80%, e.g., at least 85%, atleast 86%, at least 87%, at least 88%, at least 89%, at least 90%, atleast 91%, at least 92%, at least 93%, at least 94%, at least 95%, atleast 96%, at least 97%, at least 98%, at least 99%, or 100%.

In one embodiment, the polypeptide comprises one or more amino acidsubstitutions, and/or one or more amino acid deletions, and/or one ormore amino acid insertions or any combination thereof in between 1 and10 positions, such as 1, 2, 3, 4, 5, 6, 7, 8, 9 or 10 positions of themature polypeptide of SEQ ID NO: 8. In one embodiment, the polypeptidepreferably comprises or consists of the amino acid sequence of SEQ IDNO: 8 or an allelic variant thereof; comprises the amino acid sequenceof SEQ ID NO: 8 and a N-terminal and/or C-terminal His-tag and/orHQ-tag; or is a fragment thereof having arabinofuranosidase activity andhaving at least 90% of the length of the mature polypeptide. In anotherembodiment, the polypeptide comprises or consists of the maturepolypeptide of SEQ ID NO: 8. In another embodiment, the polypeptidecomprises or consists of amino acids 1 to 302 of SEQ ID NO: 8. In anembodiment, the polypeptide has been isolated.

In an embodiment, the composition comprises a GH62 polypeptide havingarabinofuranosidase activity having a sequence identity to SEQ ID NO: 9of at least 80%. In an embodiment, the GH62 polypeptide has a sequenceidentity to SEQ ID NO: 9 of at least 85%. In an embodiment, the GH62polypeptide has a sequence identity to SEQ ID NO: 9 of at least 86%. Inan embodiment, the GH62 polypeptide has a sequence identity to SEQ IDNO: 9 of at least 87%. In an embodiment, the GH62 polypeptide has asequence identity to SEQ ID NO: 9 of at least 88%. In an embodiment, theGH62 polypeptide has a sequence identity to SEQ ID NO: 9 of at least89%. In an embodiment, the GH62 polypeptide has a sequence identity toSEQ ID NO: 9 of at least 90%. In an embodiment, the GH62 polypeptide hasa sequence identity to SEQ ID NO: 9 of at least 91%. In an embodiment,the GH62 polypeptide has a sequence identity to SEQ ID NO: 9 of at least92%. In an embodiment, the GH62 polypeptide has a sequence identity toSEQ ID NO: 9 of at least 93%. In an embodiment, the GH62 polypeptide hasa sequence identity to SEQ ID NO: 9 of at least 94%. In an embodiment,the GH62 polypeptide has a sequence identity to SEQ ID NO: 9 of at least95%. In an embodiment, the GH62 polypeptide has a sequence identity toSEQ ID NO: 9 of at least 96%. In an embodiment, the GH62 polypeptide hasa sequence identity to SEQ ID NO: 9 of at least 97%. In an embodiment,the GH62 polypeptide has a sequence identity to SEQ ID NO: 9 of at least98%. In an embodiment, the GH62 polypeptide has a sequence identity toSEQ ID NO: 9 of at least 99%.

In one embodiment, the polypeptide comprises one or more amino acidsubstitutions, and/or one or more amino acid deletions, and/or one ormore amino acid insertions or any combination thereof in between 1 and10 positions, such as 1, 2, 3, 4, 5, 6, 7, 8, 9 or 10 positions of SEQID NO: 9. In one embodiment, the polypeptide preferably comprises orconsists of the amino acid sequence of SEQ ID NO: 9 or an allelicvariant thereof; comprises SEQ ID NO: 9 or an allelic variant thereofand a N-terminal and/or C-terminal His-tag and/or HQ-tag; or is afragment thereof having arabinofuranosidase activity and having at least90% of the length of SEQ ID NO: 9. In another embodiment, thepolypeptide comprises or consists of amino acids 1 to 302 of SEQ ID NO:9. In an embodiment, the polypeptide has been isolated.

In another embodiment, the composition comprises a GH62 polypeptidehaving arabinofuranosidase activity, wherein GH62 polypeptide havingarabinofuranosidase activity has a sequence identity to the maturepolypeptide of SEQ ID NO: 11 of at least 80%, e.g., at least 85%, atleast 86%, at least 87%, at least 88%, at least 89%, at least 90%, atleast 91%, at least 92%, at least 93%, at least 94%, at least 95%, atleast 96%, at least 97%, at least 98%, at least 99%, or 100%.

In one embodiment, the polypeptide comprises one or more amino acidsubstitutions, and/or one or more amino acid deletions, and/or one ormore amino acid insertions or any combination thereof in between 1 and10 positions, such as 1, 2, 3, 4, 5, 6, 7, 8, 9 or 10 positions of themature polypeptide of SEQ ID NO: 11. In one embodiment, the polypeptidepreferably comprises or consists of the amino acid sequence of SEQ IDNO: 11 or an allelic variant thereof; comprises the amino acid sequenceof SEQ ID NO: 11 and a N-terminal and/or C-terminal His-tag and/orHQ-tag; or is a fragment thereof having arabinofuranosidase activity andhaving at least 90% of the length of the mature polypeptide. In anotherembodiment, the polypeptide comprises or consists of the maturepolypeptide of SEQ ID NO: 11. In another embodiment, the polypeptidecomprises or consists of amino acids 1 to 303 of SEQ ID NO: 11. In anembodiment, the polypeptide has been isolated.

In an embodiment, the composition comprises a GH62 polypeptide havingarabinofuranosidase activity having a sequence identity to SEQ ID NO: 12of at least 80%. In an embodiment, the GH62 polypeptide has a sequenceidentity to SEQ ID NO: 12 of at least 85%. In an embodiment, the GH62polypeptide has a sequence identity to SEQ ID NO: 12 of at least 86%. Inan embodiment, the GH62 polypeptide has a sequence identity to SEQ IDNO: 12 of at least 87%. In an embodiment, the GH62 polypeptide has asequence identity to SEQ ID NO: 12 of at least 88%. In an embodiment,the GH62 polypeptide has a sequence identity to SEQ ID NO: 12 of atleast 89%. In an embodiment, the GH62 polypeptide has a sequenceidentity to SEQ ID NO: 12 of at least 90%. In an embodiment, the GH62polypeptide has a sequence identity to SEQ ID NO: 12 of at least 91%. Inan embodiment, the GH62 polypeptide has a sequence identity to SEQ IDNO: 12 of at least 92%. In an embodiment, the GH62 polypeptide has asequence identity to SEQ ID NO: 12 of at least 93%. In an embodiment,the GH62 polypeptide has a sequence identity to SEQ ID NO: 12 of atleast 94%. In an embodiment, the GH62 polypeptide has a sequenceidentity to SEQ ID NO: 12 of at least 95%. In an embodiment, the GH62polypeptide has a sequence identity to SEQ ID NO: 12 of at least 96%. Inan embodiment, the GH62 polypeptide has a sequence identity to SEQ IDNO: 12 of at least 97%. In an embodiment, the GH62 polypeptide has asequence identity to SEQ ID NO: 12 of at least 98%. In an embodiment,the GH62 polypeptide has a sequence identity to SEQ ID NO: 12 of atleast 99%.

In one embodiment, the polypeptide comprises one or more amino acidsubstitutions, and/or one or more amino acid deletions, and/or one ormore amino acid insertions or any combination thereof in between 1 and10 positions, such as 1, 2, 3, 4, 5, 6, 7, 8, 9 or 10 positions of SEQID NO: 12. In one embodiment, the polypeptide preferably comprises orconsists of the amino acid sequence of SEQ ID NO: 12 or an allelicvariant thereof; comprises SEQ ID NO: 12 or an allelic variant thereofand a N-terminal and/or C-terminal His-tag and/or HQ-tag; or is afragment thereof having arabinofuranosidase activity and having at least90% of the length of SEQ ID NO: 12. In another embodiment, thepolypeptide comprises or consists of amino acids 1 to 303 of SEQ ID NO:12. In an embodiment, the polypeptide has been isolated.

In another embodiment, the composition comprises a GH62 polypeptidehaving arabinofuranosidase activity, wherein GH62 polypeptide havingarabinofuranosidase activity has a sequence identity to the maturepolypeptide of SEQ ID NO: 14 of at least 80%, e.g., at least 85%, atleast 86%, at least 87%, at least 88%, at least 89%, at least 90%, atleast 91%, at least 92%, at least 93%, at least 94%, at least 95%, atleast 96%, at least 97%, at least 98%, at least 99%, or 100%.

In one embodiment, the polypeptide comprises one or more amino acidsubstitutions, and/or one or more amino acid deletions, and/or one ormore amino acid insertions or any combination thereof in between 1 and10 positions, such as 1, 2, 3, 4, 5, 6, 7, 8, 9 or 10 positions of themature polypeptide of SEQ ID NO: 14. In one embodiment, the polypeptidepreferably comprises or consists of the amino acid sequence of SEQ IDNO: 14 or an allelic variant thereof; comprises the amino acid sequenceof SEQ ID NO: 14 and a N-terminal and/or C-terminal His-tag and/orHQ-tag; or is a fragment thereof having arabinofuranosidase activity andhaving at least 90% of the length of the mature polypeptide. In anotherembodiment, the polypeptide comprises or consists of the maturepolypeptide of SEQ ID NO: 14. In another embodiment, the polypeptidecomprises or consists of amino acids 1 to 382 of SEQ ID NO: 14. In anembodiment, the polypeptide has been isolated.

In an embodiment, the composition comprises a GH62 polypeptide havingarabinofuranosidase activity having a sequence identity to SEQ ID NO: 15of at least 80%. In an embodiment, the GH62 polypeptide has a sequenceidentity to SEQ ID NO: 15 of at least 85%. In an embodiment, the GH62polypeptide has a sequence identity to SEQ ID NO: 15 of at least 86%. Inan embodiment, the GH62 polypeptide has a sequence identity to SEQ IDNO: 15 of at least 87%. In an embodiment, the GH62 polypeptide has asequence identity to SEQ ID NO: 15 of at least 88%. In an embodiment,the GH62 polypeptide has a sequence identity to SEQ ID NO: 15 of atleast 89%. In an embodiment, the GH62 polypeptide has a sequenceidentity to SEQ ID NO: 15 of at least 90%. In an embodiment, the GH62polypeptide has a sequence identity to SEQ ID NO: 15 of at least 91%. Inan embodiment, the GH62 polypeptide has a sequence identity to SEQ IDNO: 15 of at least 92%. In an embodiment, the GH62 polypeptide has asequence identity to SEQ ID NO: 15 of at least 93%. In an embodiment,the GH62 polypeptide has a sequence identity to SEQ ID NO: 15 of atleast 94%. In an embodiment, the GH62 polypeptide has a sequenceidentity to SEQ ID NO: 15 of at least 95%. In an embodiment, the GH62polypeptide has a sequence identity to SEQ ID NO: 15 of at least 96%. Inan embodiment, the GH62 polypeptide has a sequence identity to SEQ IDNO: 15 of at least 97%. In an embodiment, the GH62 polypeptide has asequence identity to SEQ ID NO: 15 of at least 98%. In an embodiment,the GH62 polypeptide has a sequence identity to SEQ ID NO: 15 of atleast 99%.

In one embodiment, the polypeptide comprises one or more amino acidsubstitutions, and/or one or more amino acid deletions, and/or one ormore amino acid insertions or any combination thereof in between 1 and10 positions, such as 1, 2, 3, 4, 5, 6, 7, 8, 9 or 10 positions of SEQID NO: 15. In one embodiment, the polypeptide preferably comprises orconsists of the amino acid sequence of SEQ ID NO: 15 or an allelicvariant thereof; comprises SEQ ID NO: 15 or an allelic variant thereofand a N-terminal and/or C-terminal His-tag and/or HQ-tag; or is afragment thereof having arabinofuranosidase activity and having at least90% of the length of SEQ ID NO: 15. In another embodiment, thepolypeptide comprises or consists of amino acids 1 to 382 of SEQ ID NO:15. In an embodiment, the polypeptide has been isolated.

In another embodiment, the composition comprises a GH62 polypeptidehaving arabinofuranosidase activity, wherein GH62 polypeptide havingarabinofuranosidase activity has a sequence identity to the maturepolypeptide of SEQ ID NO: 17 of at least 80%, e.g., at least 85%, atleast 86%, at least 87%, at least 88%, at least 89%, at least 90%, atleast 91%, at least 92%, at least 93%, at least 94%, at least 95%, atleast 96%, at least 97%, at least 98%, at least 99%, or 100%.

In one embodiment, the polypeptide comprises one or more amino acidsubstitutions, and/or one or more amino acid deletions, and/or one ormore amino acid insertions or any combination thereof in between 1 and10 positions, such as 1, 2, 3, 4, 5, 6, 7, 8, 9 or 10 positions of themature polypeptide of SEQ ID NO: 17. In one embodiment, the polypeptidepreferably comprises or consists of the amino acid sequence of SEQ IDNO: 17 or an allelic variant thereof; comprises the amino acid sequenceof SEQ ID NO: 17 and a N-terminal and/or C-terminal His-tag and/orHQ-tag; or is a fragment thereof having arabinofuranosidase activity andhaving at least 90% of the length of the mature polypeptide. In anotherembodiment, the polypeptide comprises or consists of the maturepolypeptide of SEQ ID NO: 17. In another embodiment, the polypeptidecomprises or consists of amino acids 1 to 378 of SEQ ID NO: 17. In anembodiment, the polypeptide has been isolated.

In an embodiment, the composition comprises a GH62 polypeptide havingarabinofuranosidase activity having a sequence identity to SEQ ID NO: 18of at least 80%. In an embodiment, the GH62 polypeptide has a sequenceidentity to SEQ ID NO: 18 of at least 85%. In an embodiment, the GH62polypeptide has a sequence identity to SEQ ID NO: 18 of at least 86%. Inan embodiment, the GH62 polypeptide has a sequence identity to SEQ IDNO: 18 of at least 87%. In an embodiment, the GH62 polypeptide has asequence identity to SEQ ID NO: 18 of at least 88%. In an embodiment,the GH62 polypeptide has a sequence identity to SEQ ID NO: 18 of atleast 89%. In an embodiment, the GH62 polypeptide has a sequenceidentity to SEQ ID NO: 18 of at least 90%. In an embodiment, the GH62polypeptide has a sequence identity to SEQ ID NO: 18 of at least 91%. Inan embodiment, the GH62 polypeptide has a sequence identity to SEQ IDNO: 18 of at least 92%. In an embodiment, the GH62 polypeptide has asequence identity to SEQ ID NO: 18 of at least 93%. In an embodiment,the GH62 polypeptide has a sequence identity to SEQ ID NO: 18 of atleast 94%. In an embodiment, the GH62 polypeptide has a sequenceidentity to SEQ ID NO: 18 of at least 95%. In an embodiment, the GH62polypeptide has a sequence identity to SEQ ID NO: 18 of at least 96%. Inan embodiment, the GH62 polypeptide has a sequence identity to SEQ IDNO: 18 of at least 97%. In an embodiment, the GH62 polypeptide has asequence identity to SEQ ID NO: 18 of at least 98%. In an embodiment,the GH62 polypeptide has a sequence identity to SEQ ID NO: 18 of atleast 99%.

In one embodiment, the polypeptide comprises one or more amino acidsubstitutions, and/or one or more amino acid deletions, and/or one ormore amino acid insertions or any combination thereof in between 1 and10 positions, such as 1, 2, 3, 4, 5, 6, 7, 8, 9 or 10 positions of SEQID NO: 18. In one embodiment, the polypeptide preferably comprises orconsists of the amino acid sequence of SEQ ID NO: 18 or an allelicvariant thereof; comprises SEQ ID NO: 18 or an allelic variant thereofand a N-terminal and/or C-terminal His-tag and/or HQ-tag; or is afragment thereof having arabinofuranosidase activity and having at least90% of the length of SEQ ID NO: 18. In another embodiment, thepolypeptide comprises or consists of amino acids 1 to 378 of SEQ ID NO:18. In an embodiment, the polypeptide has been isolated.

In another embodiment, the composition comprises a GH62 polypeptidehaving arabinofuranosidase activity, wherein GH62 polypeptide havingarabinofuranosidase activity has a sequence identity to the maturepolypeptide of SEQ ID NO: 20 of at least 80%, e.g., at least 85%, atleast 86%, at least 87%, at least 88%, at least 89%, at least 90%, atleast 91%, at least 92%, at least 93%, at least 94%, at least 95%, atleast 96%, at least 97%, at least 98%, at least 99%, or 100%.

In one embodiment, the polypeptide comprises one or more amino acidsubstitutions, and/or one or more amino acid deletions, and/or one ormore amino acid insertions or any combination thereof in between 1 and10 positions, such as 1, 2, 3, 4, 5, 6, 7, 8, 9 or 10 positions of themature polypeptide of SEQ ID NO: 20. In one embodiment, the polypeptidepreferably comprises or consists of the amino acid sequence of SEQ IDNO: 20 or an allelic variant thereof; comprises the amino acid sequenceof SEQ ID NO: 20 and a N-terminal and/or C-terminal His-tag and/orHQ-tag; or is a fragment thereof having arabinofuranosidase activity andhaving at least 90% of the length of the mature polypeptide. In anotherembodiment, the polypeptide comprises or consists of the maturepolypeptide of SEQ ID NO: 20. In another embodiment, the polypeptidecomprises or consists of amino acids 1 to 311 of SEQ ID NO: 20. In anembodiment, the polypeptide has been isolated.

In an embodiment, the composition comprises a GH62 polypeptide havingarabinofuranosidase activity having a sequence identity to SEQ ID NO: 21of at least 80%. In an embodiment, the GH62 polypeptide has a sequenceidentity to SEQ ID NO: 21 of at least 85%. In an embodiment, the GH62polypeptide has a sequence identity to SEQ ID NO: 21 of at least 86%. Inan embodiment, the GH62 polypeptide has a sequence identity to SEQ IDNO: 21 of at least 87%. In an embodiment, the GH62 polypeptide has asequence identity to SEQ ID NO: 21 of at least 88%. In an embodiment,the GH62 polypeptide has a sequence identity to SEQ ID NO: 21 of atleast 89%. In an embodiment, the GH62 polypeptide has a sequenceidentity to SEQ ID NO: 21 of at least 90%. In an embodiment, the GH62polypeptide has a sequence identity to SEQ ID NO: 21 of at least 91%. Inan embodiment, the GH62 polypeptide has a sequence identity to SEQ IDNO: 21 of at least 92%. In an embodiment, the GH62 polypeptide has asequence identity to SEQ ID NO: 21 of at least 93%. In an embodiment,the GH62 polypeptide has a sequence identity to SEQ ID NO: 21 of atleast 94%. In an embodiment, the GH62 polypeptide has a sequenceidentity to SEQ ID NO: 21 of at least 95%. In an embodiment, the GH62polypeptide has a sequence identity to SEQ ID NO: 21 of at least 96%. Inan embodiment, the GH62 polypeptide has a sequence identity to SEQ IDNO: 21 of at least 97%. In an embodiment, the GH62 polypeptide has asequence identity to SEQ ID NO: 21 of at least 98%. In an embodiment,the GH62 polypeptide has a sequence identity to SEQ ID NO: 21 of atleast 99%.

In one embodiment, the polypeptide comprises one or more amino acidsubstitutions, and/or one or more amino acid deletions, and/or one ormore amino acid insertions or any combination thereof in between 1 and10 positions, such as 1, 2, 3, 4, 5, 6, 7, 8, 9 or 10 positions of SEQID NO: 21. In one embodiment, the polypeptide preferably comprises orconsists of the amino acid sequence of SEQ ID NO: 21 or an allelicvariant thereof; comprises SEQ ID NO: 21 or an allelic variant thereofand a N-terminal and/or C-terminal His-tag and/or HQ-tag; or is afragment thereof having arabinofuranosidase activity and having at least90% of the length of SEQ ID NO: 21. In another embodiment, thepolypeptide comprises or consists of amino acids 1 to 311 of SEQ ID NO:21. In an embodiment, the polypeptide has been isolated.

In another embodiment, the composition comprises a GH62 polypeptidehaving arabinofuranosidase activity, wherein GH62 polypeptide havingarabinofuranosidase activity has a sequence identity to the maturepolypeptide of SEQ ID NO: 23 of at least 80%, e.g., at least 85%, atleast 86%, at least 87%, at least 88%, at least 89%, at least 90%, atleast 91%, at least 92%, at least 93%, at least 94%, at least 95%, atleast 96%, at least 97%, at least 98%, at least 99%, or 100%.

In one embodiment, the polypeptide comprises one or more amino acidsubstitutions, and/or one or more amino acid deletions, and/or one ormore amino acid insertions or any combination thereof in between 1 and10 positions, such as 1, 2, 3, 4, 5, 6, 7, 8, 9 or 10 positions of themature polypeptide of SEQ ID NO: 23. In one embodiment, the polypeptidepreferably comprises or consists of the amino acid sequence of SEQ IDNO: 23 or an allelic variant thereof; comprises the amino acid sequenceof SEQ ID NO: 23 and a N-terminal and/or C-terminal His-tag and/orHQ-tag; or is a fragment thereof having arabinofuranosidase activity andhaving at least 90% of the length of the mature polypeptide. In anotherembodiment, the polypeptide comprises or consists of the maturepolypeptide of SEQ ID NO: 23. In another embodiment, the polypeptidecomprises or consists of amino acids 1 to 302 of SEQ ID NO: 23. In anembodiment, the polypeptide has been isolated.

In an embodiment, the composition comprises a GH62 polypeptide havingarabinofuranosidase activity having a sequence identity to SEQ ID NO: 24of at least 80%. In an embodiment, the GH62 polypeptide has a sequenceidentity to SEQ ID NO: 24 of at least 85%. In an embodiment, the GH62polypeptide has a sequence identity to SEQ ID NO: 24 of at least 86%. Inan embodiment, the GH62 polypeptide has a sequence identity to SEQ IDNO: 24 of at least 87%. In an embodiment, the GH62 polypeptide has asequence identity to SEQ ID NO: 24 of at least 88%. In an embodiment,the GH62 polypeptide has a sequence identity to SEQ ID NO: 24 of atleast 89%. In an embodiment, the GH62 polypeptide has a sequenceidentity to SEQ ID NO: 24 of at least 90%. In an embodiment, the GH62polypeptide has a sequence identity to SEQ ID NO: 24 of at least 91%. Inan embodiment, the GH62 polypeptide has a sequence identity to SEQ IDNO: 24 of at least 92%. In an embodiment, the GH62 polypeptide has asequence identity to SEQ ID NO: 24 of at least 93%. In an embodiment,the GH62 polypeptide has a sequence identity to SEQ ID NO: 24 of atleast 94%. In an embodiment, the GH62 polypeptide has a sequenceidentity to SEQ ID NO: 24 of at least 95%. In an embodiment, the GH62polypeptide has a sequence identity to SEQ ID NO: 24 of at least 96%. Inan embodiment, the GH62 polypeptide has a sequence identity to SEQ IDNO: 24 of at least 97%. In an embodiment, the GH62 polypeptide has asequence identity to SEQ ID NO: 24 of at least 98%. In an embodiment,the GH62 polypeptide has a sequence identity to SEQ ID NO: 24 of atleast 99%.

In one embodiment, the polypeptide comprises one or more amino acidsubstitutions, and/or one or more amino acid deletions, and/or one ormore amino acid insertions or any combination thereof in between 1 and10 positions, such as 1, 2, 3, 4, 5, 6, 7, 8, 9 or 10 positions of SEQID NO: 24. In one embodiment, the polypeptide preferably comprises orconsists of the amino acid sequence of SEQ ID NO: 24 or an allelicvariant thereof; comprises SEQ ID NO: 24 or an allelic variant thereofand a N-terminal and/or C-terminal His-tag and/or HQ-tag; or is afragment thereof having arabinofuranosidase activity and having at least90% of the length of SEQ ID NO: 24. In another embodiment, thepolypeptide comprises or consists of amino acids 1 to 302 of SEQ ID NO:24. In an embodiment, the polypeptide has been isolated.

In another embodiment, the composition comprises a GH62 polypeptidehaving arabinofuranosidase activity, wherein GH62 polypeptide havingarabinofuranosidase activity has a sequence identity to the maturepolypeptide of SEQ ID NO: 26 of at least 80%, e.g., at least 85%, atleast 86%, at least 87%, at least 88%, at least 89%, at least 90%, atleast 91%, at least 92%, at least 93%, at least 94%, at least 95%, atleast 96%, at least 97%, at least 98%, at least 99%, or 100%.

In one embodiment, the polypeptide comprises one or more amino acidsubstitutions, and/or one or more amino acid deletions, and/or one ormore amino acid insertions or any combination thereof in between 1 and10 positions, such as 1, 2, 3, 4, 5, 6, 7, 8, 9 or 10 positions of themature polypeptide of SEQ ID NO: 26. In one embodiment, the polypeptidepreferably comprises or consists of the amino acid sequence of SEQ IDNO: 26 or an allelic variant thereof; comprises the amino acid sequenceof SEQ ID NO: 26 and a N-terminal and/or C-terminal His-tag and/orHQ-tag; or is a fragment thereof having arabinofuranosidase activity andhaving at least 90% of the length of the mature polypeptide. In anotherembodiment, the polypeptide comprises or consists of the maturepolypeptide of SEQ ID NO: 26. In another embodiment, the polypeptidecomprises or consists of amino acids 1 to 309 of SEQ ID NO: 26. In anembodiment, the polypeptide has been isolated.

In an embodiment, the composition comprises a GH62 polypeptide havingarabinofuranosidase activity having a sequence identity to SEQ ID NO: 27of at least 80%. In an embodiment, the GH62 polypeptide has a sequenceidentity to SEQ ID NO: 27 of at least 85%.

In an embodiment, the GH62 polypeptide has a sequence identity to SEQ IDNO: 27 of at least 86%. In an embodiment, the GH62 polypeptide has asequence identity to SEQ ID NO: 27 of at least 87%. In an embodiment,the GH62 polypeptide has a sequence identity to SEQ ID NO: 27 of atleast 88%. In an embodiment, the GH62 polypeptide has a sequenceidentity to SEQ ID NO: 27 of at least 89%. In an embodiment, the GH62polypeptide has a sequence identity to SEQ ID NO: 27 of at least 90%. Inan embodiment, the GH62 polypeptide has a sequence identity to SEQ IDNO: 27 of at least 91%. In an embodiment, the GH62 polypeptide has asequence identity to SEQ ID NO: 27 of at least 92%. In an embodiment,the GH62 polypeptide has a sequence identity to SEQ ID NO: 27 of atleast 93%. In an embodiment, the GH62 polypeptide has a sequenceidentity to SEQ ID NO: 27 of at least 94%. In an embodiment, the GH62polypeptide has a sequence identity to SEQ ID NO: 27 of at least 95%. Inan embodiment, the GH62 polypeptide has a sequence identity to SEQ IDNO: 27 of at least 96%. In an embodiment, the GH62 polypeptide has asequence identity to SEQ ID NO: 27 of at least 97%. In an embodiment,the GH62 polypeptide has a sequence identity to SEQ ID NO: 27 of atleast 98%. In an embodiment, the GH62 polypeptide has a sequenceidentity to SEQ ID NO: 27 of at least 99%.

In one embodiment, the polypeptide comprises one or more amino acidsubstitutions, and/or one or more amino acid deletions, and/or one ormore amino acid insertions or any combination thereof in between 1 and10 positions, such as 1, 2, 3, 4, 5, 6, 7, 8, 9 or 10 positions of SEQID NO: 27. In one embodiment, the polypeptide preferably comprises orconsists of the amino acid sequence of SEQ ID NO: 27 or an allelicvariant thereof; comprises SEQ ID NO: 27 or an allelic variant thereofand a N-terminal and/or C-terminal His-tag and/or HQ-tag; or is afragment thereof having arabinofuranosidase activity and having at least90% of the length of SEQ ID NO: 27. In another embodiment, thepolypeptide comprises or consists of amino acids 1 to 309 of SEQ ID NO:27. In an embodiment, the polypeptide has been isolated.

In another embodiment, the composition comprises a GH62 polypeptidehaving arabinofuranosidase activity, wherein GH62 polypeptide havingarabinofuranosidase activity has a sequence identity to the maturepolypeptide of SEQ ID NO: 29 of at least 80%, e.g., at least 85%, atleast 86%, at least 87%, at least 88%, at least 89%, at least 90%, atleast 91%, at least 92%, at least 93%, at least 94%, at least 95%, atleast 96%, at least 97%, at least 98%, at least 99%, or 100%.

In one embodiment, the polypeptide comprises one or more amino acidsubstitutions, and/or one or more amino acid deletions, and/or one ormore amino acid insertions or any combination thereof in between 1 and10 positions, such as 1, 2, 3, 4, 5, 6, 7, 8, 9 or 10 positions of themature polypeptide of SEQ ID NO: 29. In one embodiment, the polypeptidepreferably comprises or consists of the amino acid sequence of SEQ IDNO: 29 or an allelic variant thereof; comprises the amino acid sequenceof SEQ ID NO: 29 and a N-terminal and/or C-terminal His-tag and/orHQ-tag such as the mature polypeptide of SEQ ID NO: 32 or SEQ ID NO: 33;or is a fragment thereof having arabinofuranosidase activity and havingat least 90% of the length of the mature polypeptide. In anotherembodiment, the polypeptide comprises or consists of the maturepolypeptide of SEQ ID NO: 29. In another embodiment, the polypeptidecomprises or consists of amino acids 1 to 438 of SEQ ID NO: 29. Inanother embodiment, the polypeptide comprises or consists of the maturepolypeptide of SEQ ID NO: 32. In another embodiment, the polypeptidecomprises or consists of amino acids 1 to 446 of SEQ ID NO: 32. In anembodiment, the polypeptide has been isolated.

In an embodiment, the composition comprises a GH62 polypeptide havingarabinofuranosidase activity having a sequence identity to SEQ ID NO: 30of at least 80%. In an embodiment, the GH62 polypeptide has a sequenceidentity to SEQ ID NO: 30 of at least 85%. In an embodiment, the GH62polypeptide has a sequence identity to SEQ ID NO: 30 of at least 86%. Inan embodiment, the GH62 polypeptide has a sequence identity to SEQ IDNO: 30 of at least 87%. In an embodiment, the GH62 polypeptide has asequence identity to SEQ ID NO: 30 of at least 88%. In an embodiment,the GH62 polypeptide has a sequence identity to SEQ ID NO: 30 of atleast 89%. In an embodiment, the GH62 polypeptide has a sequenceidentity to SEQ ID NO: 30 of at least 90%. In an embodiment, the GH62polypeptide has a sequence identity to SEQ ID NO: 30 of at least 91%. Inan embodiment, the GH62 polypeptide has a sequence identity to SEQ IDNO: 30 of at least 92%. In an embodiment, the GH62 polypeptide has asequence identity to SEQ ID NO: 30 of at least 93%. In an embodiment,the GH62 polypeptide has a sequence identity to SEQ ID NO: 30 of atleast 94%. In an embodiment, the GH62 polypeptide has a sequenceidentity to SEQ ID NO: 30 of at least 95%. In an embodiment, the GH62polypeptide has a sequence identity to SEQ ID NO: 30 of at least 96%. Inan embodiment, the GH62 polypeptide has a sequence identity to SEQ IDNO: 30 of at least 97%. In an embodiment, the GH62 polypeptide has asequence identity to SEQ ID NO: 30 of at least 98%. In an embodiment,the GH62 polypeptide has a sequence identity to SEQ ID NO: 30 of atleast 99%.

In one embodiment, the polypeptide comprises one or more amino acidsubstitutions, and/or one or more amino acid deletions, and/or one ormore amino acid insertions or any combination thereof in between 1 and10 positions, such as 1, 2, 3, 4, 5, 6, 7, 8, 9 or 10 positions of SEQID NO: 30. In one embodiment, the polypeptide comprises one or moreamino acid substitutions, and/or one or more amino acid deletions,and/or one or more amino acid insertions or any combination thereof inbetween 1 and 10 positions, such as 1, 2, 3, 4, 5, 6, 7, 8, 9 or 10positions of SEQ ID NO: 33. In one embodiment, the polypeptidepreferably comprises or consists of the amino acid sequence of SEQ IDNO: 30 or an allelic variant thereof; comprises SEQ ID NO: 30 or anallelic variant thereof and a N-terminal and/or C-terminal His-tagand/or HQ-tag such as SEQ ID NO: 33; or is a fragment thereof havingarabinofuranosidase activity and having at least 90% of the length ofSEQ ID NO: 30. In another embodiment, the polypeptide comprises orconsists of amino acids 1 to 438 of SEQ ID NO: 30. In anotherembodiment, the polypeptide comprises or consists of amino acids 1 to446 of SEQ ID NO: 33. In an embodiment, the polypeptide has beenisolated.

In another embodiment, the composition comprises a GH62 polypeptidehaving arabinofuranosidase activity, wherein GH62 polypeptide havingarabinofuranosidase activity has a sequence identity to the maturepolypeptide of SEQ ID NO: 35 of at least 80%, e.g., at least 85%, atleast 86%, at least 87%, at least 88%, at least 89%, at least 90%, atleast 91%, at least 92%, at least 93%, at least 94%, at least 95%, atleast 96%, at least 97%, at least 98%, at least 99%, or 100%.

In one embodiment, the polypeptide comprises one or more amino acidsubstitutions, and/or one or more amino acid deletions, and/or one ormore amino acid insertions or any combination thereof in between 1 and10 positions, such as 1, 2, 3, 4, 5, 6, 7, 8, 9 or 10 positions of themature polypeptide of SEQ ID NO: 35. In one embodiment, the polypeptidepreferably comprises or consists of the amino acid sequence of SEQ IDNO: 35 or an allelic variant thereof; comprises the amino acid sequenceof SEQ ID NO: 35 and a N-terminal and/or C-terminal His-tag and/orHQ-tag such as the mature polypeptide of SEQ ID NO: 38 or SEQ ID NO: 39;or is a fragment thereof having arabinofuranosidase activity and havingat least 90% of the length of the mature polypeptide. In anotherembodiment, the polypeptide comprises or consists of the maturepolypeptide of SEQ ID NO: 35. In another embodiment, the polypeptidecomprises or consists of amino acids 1 to 438 of SEQ ID NO: 35. Inanother embodiment, the polypeptide comprises or consists of the maturepolypeptide of SEQ ID NO: 38. In another embodiment, the polypeptidecomprises or consists of amino acids 1 to 446 of SEQ ID NO: 38. In anembodiment, the polypeptide has been isolated.

In an embodiment, the composition comprises a GH62 polypeptide havingarabinofuranosidase activity having a sequence identity to SEQ ID NO: 36of at least 80%. In an embodiment, the GH62 polypeptide has a sequenceidentity to SEQ ID NO: 36 of at least 85%. In an embodiment, the GH62polypeptide has a sequence identity to SEQ ID NO: 36 of at least 86%. Inan embodiment, the GH62 polypeptide has a sequence identity to SEQ IDNO: 36 of at least 87%. In an embodiment, the GH62 polypeptide has asequence identity to SEQ ID NO: 36 of at least 88%. In an embodiment,the GH62 polypeptide has a sequence identity to SEQ ID NO: 36 of atleast 89%. In an embodiment, the GH62 polypeptide has a sequenceidentity to SEQ ID NO: 36 of at least 90%. In an embodiment, the GH62polypeptide has a sequence identity to SEQ ID NO: 36 of at least 91%. Inan embodiment, the GH62 polypeptide has a sequence identity to SEQ IDNO: 36 of at least 92%. In an embodiment, the GH62 polypeptide has asequence identity to SEQ ID NO: 36 of at least 93%. In an embodiment,the GH62 polypeptide has a sequence identity to SEQ ID NO: 36 of atleast 94%. In an embodiment, the GH62 polypeptide has a sequenceidentity to SEQ ID NO: 36 of at least 95%. In an embodiment, the GH62polypeptide has a sequence identity to SEQ ID NO: 36 of at least 96%. Inan embodiment, the GH62 polypeptide has a sequence identity to SEQ IDNO: 36 of at least 97%. In an embodiment, the GH62 polypeptide has asequence identity to SEQ ID NO: 36 of at least 98%. In an embodiment,the GH62 polypeptide has a sequence identity to SEQ ID NO: 36 of atleast 99%.

In one embodiment, the polypeptide comprises one or more amino acidsubstitutions, and/or one or more amino acid deletions, and/or one ormore amino acid insertions or any combination thereof in between 1 and10 positions, such as 1, 2, 3, 4, 5, 6, 7, 8, 9 or 10 positions of SEQID NO: 36. In one embodiment, the polypeptide comprises one or moreamino acid substitutions, and/or one or more amino acid deletions,and/or one or more amino acid insertions or any combination thereof inbetween 1 and 10 positions, such as 1, 2, 3, 4, 5, 6, 7, 8, 9 or 10positions of SEQ ID NO: 39. In one embodiment, the polypeptidepreferably comprises or consists of the amino acid sequence of SEQ IDNO: 36 or an allelic variant thereof; comprises SEQ ID NO: 36 or anallelic variant thereof and a N-terminal and/or C-terminal His-tagand/or HQ-tag such as SEQ ID NO: 39; or is a fragment thereof havingarabinofuranosidase activity and having at least 90% of the length ofSEQ ID NO: 36. In another embodiment, the polypeptide comprises orconsists of amino acids 1 to 438 of SEQ ID NO: 36. In anotherembodiment, the polypeptide comprises or consists of amino acids 1 to446 of SEQ ID NO: 39. In an embodiment, the polypeptide has beenisolated.

In another embodiment, the composition comprises a GH62 polypeptidehaving arabinofuranosidase activity, wherein GH62 polypeptide havingarabinofuranosidase activity has a sequence identity to the maturepolypeptide of SEQ ID NO: 41 of at least 80%, e.g., at least 85%, atleast 86%, at least 87%, at least 88%, at least 89%, at least 90%, atleast 91%, at least 92%, at least 93%, at least 94%, at least 95%, atleast 96%, at least 97%, at least 98%, at least 99%, or 100%.

In one embodiment, the polypeptide comprises one or more amino acidsubstitutions, and/or one or more amino acid deletions, and/or one ormore amino acid insertions or any combination thereof in between 1 and10 positions, such as 1, 2, 3, 4, 5, 6, 7, 8, 9 or 10 positions of themature polypeptide of SEQ ID NO: 41. In one embodiment, the polypeptidepreferably comprises or consists of the amino acid sequence of SEQ IDNO: 41 or an allelic variant thereof; comprises the amino acid sequenceof SEQ ID NO: 41 and a N-terminal and/or C-terminal His-tag and/orHQ-tag such as the mature polypeptide of SEQ ID NO: 44 or SEQ ID NO: 45;or is a fragment thereof having arabinofuranosidase activity and havingat least 90% of the length of the mature polypeptide. In anotherembodiment, the polypeptide comprises or consists of the maturepolypeptide of SEQ ID NO: 41. In another embodiment, the polypeptidecomprises or consists of amino acids 1 to 318 of SEQ ID NO: 41. Inanother embodiment, the polypeptide comprises or consists of the maturepolypeptide of SEQ ID NO: 44. In another embodiment, the polypeptidecomprises or consists of amino acids 1 to 326 of SEQ ID NO: 44. In anembodiment, the polypeptide has been isolated.

In an embodiment, the composition comprises a GH62 polypeptide havingarabinofuranosidase activity having a sequence identity to SEQ ID NO: 42of at least 80%. In an embodiment, the GH62 polypeptide has a sequenceidentity to SEQ ID NO: 42 of at least 85%. In an embodiment, the GH62polypeptide has a sequence identity to SEQ ID NO: 42 of at least 86%. Inan embodiment, the GH62 polypeptide has a sequence identity to SEQ IDNO: 42 of at least 87%. In an embodiment, the GH62 polypeptide has asequence identity to SEQ ID NO: 42 of at least 88%. In an embodiment,the GH62 polypeptide has a sequence identity to SEQ ID NO: 42 of atleast 89%. In an embodiment, the GH62 polypeptide has a sequenceidentity to SEQ ID NO: 42 of at least 90%. In an embodiment, the GH62polypeptide has a sequence identity to SEQ ID NO: 42 of at least 91%. Inan embodiment, the GH62 polypeptide has a sequence identity to SEQ IDNO: 42 of at least 92%. In an embodiment, the GH62 polypeptide has asequence identity to SEQ ID NO: 42 of at least 93%. In an embodiment,the GH62 polypeptide has a sequence identity to SEQ ID NO: 42 of atleast 94%. In an embodiment, the GH62 polypeptide has a sequenceidentity to SEQ ID NO: 42 of at least 95%. In an embodiment, the GH62polypeptide has a sequence identity to SEQ ID NO: 42 of at least 96%. Inan embodiment, the GH62 polypeptide has a sequence identity to SEQ IDNO: 42 of at least 97%. In an embodiment, the GH62 polypeptide has asequence identity to SEQ ID NO: 42 of at least 98%. In an embodiment,the GH62 polypeptide has a sequence identity to SEQ ID NO: 42 of atleast 99%.

In one embodiment, the polypeptide comprises one or more amino acidsubstitutions, and/or one or more amino acid deletions, and/or one ormore amino acid insertions or any combination thereof in between 1 and10 positions, such as 1, 2, 3, 4, 5, 6, 7, 8, 9 or 10 positions of SEQID NO: 42. In one embodiment, the polypeptide comprises one or moreamino acid substitutions, and/or one or more amino acid deletions,and/or one or more amino acid insertions or any combination thereof inbetween 1 and 10 positions, such as 1, 2, 3, 4, 5, 6, 7, 8, 9 or 10positions of SEQ ID NO: 45. In one embodiment, the polypeptidepreferably comprises or consists of the amino acid sequence of SEQ IDNO: 42 or an allelic variant thereof; comprises SEQ ID NO: 42 or anallelic variant thereof and a N-terminal and/or C-terminal His-tagand/or HQ-tag such as SEQ ID NO: 45; or is a fragment thereof havingarabinofuranosidase activity and having at least 90% of the length ofSEQ ID NO: 42. In another embodiment, the polypeptide comprises orconsists of amino acids 1 to 318 of SEQ ID NO: 42. In anotherembodiment, the polypeptide comprises or consists of amino acids 1 to326 of SEQ ID NO: 45. In an embodiment, the polypeptide has beenisolated.

In another embodiment, the composition comprises a GH62 polypeptidehaving arabinofuranosidase activity, wherein GH62 polypeptide havingarabinofuranosidase activity has a sequence identity to the maturepolypeptide of SEQ ID NO: 47 of at least 80%, e.g., at least 85%, atleast 86%, at least 87%, at least 88%, at least 89%, at least 90%, atleast 91%, at least 92%, at least 93%, at least 94%, at least 95%, atleast 96%, at least 97%, at least 98%, at least 99%, or 100%.

In one embodiment, the polypeptide comprises one or more amino acidsubstitutions, and/or one or more amino acid deletions, and/or one ormore amino acid insertions or any combination thereof in between 1 and10 positions, such as 1, 2, 3, 4, 5, 6, 7, 8, 9 or 10 positions of themature polypeptide of SEQ ID NO: 47. In one embodiment, the polypeptidepreferably comprises or consists of the amino acid sequence of SEQ IDNO: 47 or an allelic variant thereof; comprises the amino acid sequenceof SEQ ID NO: 47 and a N-terminal and/or C-terminal His-tag and/orHQ-tag such as the mature polypeptide of SEQ ID NO: 50 or SEQ ID NO: 51;or is a fragment thereof having arabinofuranosidase activity and havingat least 90% of the length of the mature polypeptide. In anotherembodiment, the polypeptide comprises or consists of the maturepolypeptide of SEQ ID NO: 47. In another embodiment, the polypeptidecomprises or consists of amino acids 1 to 302 of SEQ ID NO: 47. Inanother embodiment, the polypeptide comprises or consists of the maturepolypeptide of SEQ ID NO: 50. In another embodiment, the polypeptidecomprises or consists of amino acids 1 to 311 of SEQ ID NO: 50. In anembodiment, the polypeptide has been isolated.

In an embodiment, the composition comprises a GH62 polypeptide havingarabinofuranosidase activity having a sequence identity to SEQ ID NO: 48of at least 80%. In an embodiment, the GH62 polypeptide has a sequenceidentity to SEQ ID NO: 48 of at least 85%. In an embodiment, the GH62polypeptide has a sequence identity to SEQ ID NO: 48 of at least 86%. Inan embodiment, the GH62 polypeptide has a sequence identity to SEQ IDNO: 48 of at least 87%. In an embodiment, the GH62 polypeptide has asequence identity to SEQ ID NO: 48 of at least 88%. In an embodiment,the GH62 polypeptide has a sequence identity to SEQ ID NO: 48 of atleast 89%. In an embodiment, the GH62 polypeptide has a sequenceidentity to

SEQ ID NO: 48 of at least 90%. In an embodiment, the GH62 polypeptidehas a sequence identity to SEQ ID NO: 48 of at least 91%. In anembodiment, the GH62 polypeptide has a sequence identity to SEQ ID NO:48 of at least 92%. In an embodiment, the GH62 polypeptide has asequence identity to SEQ ID NO: 48 of at least 93%. In an embodiment,the GH62 polypeptide has a sequence identity to SEQ ID NO: 48 of atleast 94%. In an embodiment, the GH62 polypeptide has a sequenceidentity to SEQ ID NO: 48 of at least 95%. In an embodiment, the GH62polypeptide has a sequence identity to SEQ ID NO: 48 of at least 96%. Inan embodiment, the GH62 polypeptide has a sequence identity to SEQ IDNO: 48 of at least 97%. In an embodiment, the GH62 polypeptide has asequence identity to SEQ ID NO: 48 of at least 98%. In an embodiment,the GH62 polypeptide has a sequence identity to SEQ ID NO: 48 of atleast 99%.

In one embodiment, the polypeptide comprises one or more amino acidsubstitutions, and/or one or more amino acid deletions, and/or one ormore amino acid insertions or any combination thereof in between 1 and10 positions, such as 1, 2, 3, 4, 5, 6, 7, 8, 9 or 10 positions of SEQID NO: 48. In one embodiment, the polypeptide comprises one or moreamino acid substitutions, and/or one or more amino acid deletions,and/or one or more amino acid insertions or any combination thereof inbetween 1 and 10 positions, such as 1, 2, 3, 4, 5, 6, 7, 8, 9 or 10positions of SEQ ID NO: 51. In one embodiment, the polypeptidepreferably comprises or consists of the amino acid sequence of SEQ IDNO: 48 or an allelic variant thereof; comprises SEQ ID NO: 48 or anallelic variant thereof and a N-terminal and/or C-terminal His-tagand/or HQ-tag such as SEQ ID NO: 51; or is a fragment thereof havingarabinofuranosidase activity and having at least 90% of the length ofSEQ ID NO: 48. In another embodiment, the polypeptide comprises orconsists of amino acids 1 to 302 of SEQ ID NO: 48. In anotherembodiment, the polypeptide comprises or consists of amino acids 1 to311 of SEQ ID NO: 51. In an embodiment, the polypeptide has beenisolated.

In another embodiment, the composition comprises a GH62 polypeptidehaving arabinofuranosidase activity, wherein GH62 polypeptide havingarabinofuranosidase activity has a sequence identity to the maturepolypeptide of SEQ ID NO: 53 of at least 80%, e.g., at least 85%, atleast 86%, at least 87%, at least 88%, at least 89%, at least 90%, atleast 91%, at least 92%, at least 93%, at least 94%, at least 95%, atleast 96%, at least 97%, at least 98%, at least 99%, or 100%.

In one embodiment, the polypeptide comprises one or more amino acidsubstitutions, and/or one or more amino acid deletions, and/or one ormore amino acid insertions or any combination thereof in between 1 and10 positions, such as 1, 2, 3, 4, 5, 6, 7, 8, 9 or 10 positions of themature polypeptide of SEQ ID NO: 53. In one embodiment, the polypeptidepreferably comprises or consists of the amino acid sequence of SEQ IDNO: 53 or an allelic variant thereof; comprises the amino acid sequenceof SEQ ID NO: 53 and a N-terminal and/or C-terminal His-tag and/orHQ-tag such as the mature polypeptide of SEQ ID NO: 56 or SEQ ID NO: 57;or is a fragment thereof having arabinofuranosidase activity and havingat least 90% of the length of the mature polypeptide. In anotherembodiment, the polypeptide comprises or consists of the maturepolypeptide of SEQ ID NO: 53. In another embodiment, the polypeptidecomprises or consists of amino acids 1 to 364 of SEQ ID NO: 53. Inanother embodiment, the polypeptide comprises or consists of the maturepolypeptide of SEQ ID NO: 56. In another embodiment, the polypeptidecomprises or consists of amino acids 1 to 373 of SEQ ID NO: 56. In anembodiment, the polypeptide has been isolated.

In an embodiment, the composition comprises a GH62 polypeptide havingarabinofuranosidase activity having a sequence identity to SEQ ID NO: 54of at least 80%. In an embodiment, the GH62 polypeptide has a sequenceidentity to SEQ ID NO: 54 of at least 85%. In an embodiment, the GH62polypeptide has a sequence identity to SEQ ID NO: 54 of at least 86%. Inan embodiment, the GH62 polypeptide has a sequence identity to SEQ IDNO: 54 of at least 87%. In an embodiment, the GH62 polypeptide has asequence identity to SEQ ID NO: 54 of at least 88%. In an embodiment,the GH62 polypeptide has a sequence identity to SEQ ID NO: 54 of atleast 89%. In an embodiment, the GH62 polypeptide has a sequenceidentity to SEQ ID NO: 54 of at least 90%. In an embodiment, the GH62polypeptide has a sequence identity to SEQ ID NO: 54 of at least 91%. Inan embodiment, the GH62 polypeptide has a sequence identity to SEQ IDNO: 54 of at least 92%. In an embodiment, the GH62 polypeptide has asequence identity to SEQ ID NO: 54 of at least 93%. In an embodiment,the GH62 polypeptide has a sequence identity to SEQ ID NO: 54 of atleast 94%. In an embodiment, the GH62 polypeptide has a sequenceidentity to SEQ ID NO: 54 of at least 95%. In an embodiment, the GH62polypeptide has a sequence identity to SEQ ID NO: 54 of at least 96%. Inan embodiment, the GH62 polypeptide has a sequence identity to SEQ IDNO: 54 of at least 97%. In an embodiment, the GH62 polypeptide has asequence identity to SEQ ID NO: 54 of at least 98%. In an embodiment,the GH62 polypeptide has a sequence identity to SEQ ID NO: 54 of atleast 99%.

In one embodiment, the polypeptide comprises one or more amino acidsubstitutions, and/or one or more amino acid deletions, and/or one ormore amino acid insertions or any combination thereof in between 1 and10 positions, such as 1, 2, 3, 4, 5, 6, 7, 8, 9 or 10 positions of SEQID NO: 54. In one embodiment, the polypeptide comprises one or moreamino acid substitutions, and/or one or more amino acid deletions,and/or one or more amino acid insertions or any combination thereof inbetween 1 and 10 positions, such as 1, 2, 3, 4, 5, 6, 7, 8, 9 or 10positions of SEQ ID NO: 57. In one embodiment, the polypeptidepreferably comprises or consists of the amino acid sequence of SEQ IDNO: 54 or an allelic variant thereof; comprises SEQ ID NO: 54 or anallelic variant thereof and a N-terminal and/or C-terminal His-tagand/or HQ-tag such as SEQ ID NO: 57; or is a fragment thereof havingarabinofuranosidase activity and having at least 90% of the length ofSEQ ID NO: 54. In another embodiment, the polypeptide comprises orconsists of amino acids 1 to 364 of SEQ ID NO: 54. In anotherembodiment, the polypeptide comprises or consists of amino acids 1 to373 of SEQ ID NO: 57. In an embodiment, the polypeptide has beenisolated.

In another embodiment, the composition comprises a GH62 polypeptidehaving arabinofuranosidase activity, wherein GH62 polypeptide havingarabinofuranosidase activity has a sequence identity to the maturepolypeptide of SEQ ID NO: 59 of at least 80%, e.g., at least 85%, atleast 86%, at least 87%, at least 88%, at least 89%, at least 90%, atleast 91%, at least 92%, at least 93%, at least 94%, at least 95%, atleast 96%, at least 97%, at least 98%, at least 99%, or 100%.

In one embodiment, the polypeptide comprises one or more amino acidsubstitutions, and/or one or more amino acid deletions, and/or one ormore amino acid insertions or any combination thereof in between 1 and10 positions, such as 1, 2, 3, 4, 5, 6, 7, 8, 9 or 10 positions of themature polypeptide of SEQ ID NO: 59. In one embodiment, the polypeptidepreferably comprises or consists of the amino acid sequence of SEQ IDNO: 65 or an allelic variant thereof; comprises the amino acid sequenceof SEQ ID NO: 59 and a N-terminal and/or C-terminal His-tag and/orHQ-tag such as the mature polypeptide of SEQ ID NO: 62 or SEQ ID NO: 63;or is a fragment thereof having arabinofuranosidase activity and havingat least 90% of the length of the mature polypeptide. In anotherembodiment, the polypeptide comprises or consists of the maturepolypeptide of SEQ ID NO: 59. In another embodiment, the polypeptidecomprises or consists of amino acids 1 to 436 of SEQ ID NO: 59. Inanother embodiment, the polypeptide comprises or consists of the maturepolypeptide of SEQ ID NO: 62. In another embodiment, the polypeptidecomprises or consists of amino acids 1 to 444 of SEQ ID NO: 62. In anembodiment, the polypeptide has been isolated.

In an embodiment, the composition comprises a GH62 polypeptide havingarabinofuranosidase activity having a sequence identity to SEQ ID NO: 60of at least 80%. In an embodiment, the GH62 polypeptide has a sequenceidentity to SEQ ID NO: 60 of at least 85%. In an embodiment, the GH62polypeptide has a sequence identity to SEQ ID NO: 60 of at least 86%. Inan embodiment, the GH62 polypeptide has a sequence identity to SEQ IDNO: 60 of at least 87%. In an embodiment, the GH62 polypeptide has asequence identity to SEQ ID NO: 60 of at least 88%. In an embodiment,the GH62 polypeptide has a sequence identity to SEQ ID NO: 60 of atleast 89%. In an embodiment, the GH62 polypeptide has a sequenceidentity to SEQ ID NO: 60 of at least 90%. In an embodiment, the GH62polypeptide has a sequence identity to SEQ ID NO: 60 of at least 91%. Inan embodiment, the GH62 polypeptide has a sequence identity to SEQ IDNO: 60 of at least 92%. In an embodiment, the GH62 polypeptide has asequence identity to SEQ ID NO: 60 of at least 93%. In an embodiment,the GH62 polypeptide has a sequence identity to SEQ ID NO: 60 of atleast 94%. In an embodiment, the GH62 polypeptide has a sequenceidentity to SEQ ID NO: 60 of at least 95%. In an embodiment, the GH62polypeptide has a sequence identity to SEQ ID NO: 60 of at least 96%. Inan embodiment, the GH62 polypeptide has a sequence identity to SEQ IDNO: 60 of at least 97%. In an embodiment, the GH62 polypeptide has asequence identity to SEQ ID NO: 60 of at least 98%. In an embodiment,the GH62 polypeptide has a sequence identity to SEQ ID NO: 60 of atleast 99%.

In one embodiment, the polypeptide comprises one or more amino acidsubstitutions, and/or one or more amino acid deletions, and/or one ormore amino acid insertions or any combination thereof in between 1 and10 positions, such as 1, 2, 3, 4, 5, 6, 7, 8, 9 or 10 positions of SEQID NO: 60. In one embodiment, the polypeptide comprises one or moreamino acid substitutions, and/or one or more amino acid deletions,and/or one or more amino acid insertions or any combination thereof inbetween 1 and 10 positions, such as 1, 2, 3, 4, 5, 6, 7, 8, 9 or 10positions of SEQ ID NO: 63. In one embodiment, the polypeptidepreferably comprises or consists of the amino acid sequence of SEQ IDNO: 60 or an allelic variant thereof; comprises SEQ ID NO: 60 or anallelic variant thereof and a N-terminal and/or C-terminal His-tagand/or HQ-tag such as SEQ ID NO: 63; or is a fragment thereof havingarabinofuranosidase activity and having at least 90% of the length ofSEQ ID NO: 60. In another embodiment, the polypeptide comprises orconsists of amino acids 1 to 436 of SEQ ID NO: 60. In anotherembodiment, the polypeptide comprises or consists of amino acids 1 to444 of SEQ ID NO: 63. In an embodiment, the polypeptide has beenisolated.

In another embodiment, the composition comprises a GH62 polypeptidehaving arabinofuranosidase activity, wherein GH62 polypeptide havingarabinofuranosidase activity has a sequence identity to the maturepolypeptide of SEQ ID NO: 65 of at least 80%, e.g., at least 85%, atleast 86%, at least 87%, at least 88%, at least 89%, at least 90%, atleast 91%, at least 92%, at least 93%, at least 94%, at least 95%, atleast 96%, at least 97%, at least 98%, at least 99%, or 100%.

In one embodiment, the polypeptide comprises one or more amino acidsubstitutions, and/or one or more amino acid deletions, and/or one ormore amino acid insertions or any combination thereof in between 1 and10 positions, such as 1, 2, 3, 4, 5, 6, 7, 8, 9 or 10 positions of themature polypeptide of SEQ ID NO: 65. In one embodiment, the polypeptidepreferably comprises or consists of the amino acid sequence of SEQ IDNO: 65 or an allelic variant thereof; comprises the amino acid sequenceof SEQ ID NO: 65 and a N-terminal and/or C-terminal His-tag and/orHQ-tag such as the mature polypeptide of SEQ ID NO: 68 or SEQ ID NO: 69;or is a fragment thereof having arabinofuranosidase activity and havingat least 90% of the length of the mature polypeptide. In anotherembodiment, the polypeptide comprises or consists of the maturepolypeptide of SEQ ID NO: 65. In another embodiment, the polypeptidecomprises or consists of amino acids 1 to 302 of SEQ ID NO: 65. Inanother embodiment, the polypeptide comprises or consists of the maturepolypeptide of SEQ ID NO: 68. In another embodiment, the polypeptidecomprises or consists of amino acids 1 to 311 of SEQ ID NO: 68. In anembodiment, the polypeptide has been isolated.

In an embodiment, the composition comprises a GH62 polypeptide havingarabinofuranosidase activity having a sequence identity to SEQ ID NO: 66of at least 80%. In an embodiment, the GH62 polypeptide has a sequenceidentity to SEQ ID NO: 66 of at least 85%. In an embodiment, the GH62polypeptide has a sequence identity to SEQ ID NO: 66 of at least 86%. Inan embodiment, the GH62 polypeptide has a sequence identity to SEQ IDNO: 66 of at least 87%. In an embodiment, the GH62 polypeptide has asequence identity to SEQ ID NO: 66 of at least 88%. In an embodiment,the GH62 polypeptide has a sequence identity to SEQ ID NO: 66 of atleast 89%. In an embodiment, the GH62 polypeptide has a sequenceidentity to SEQ ID NO: 66 of at least 90%. In an embodiment, the GH62polypeptide has a sequence identity to SEQ ID NO: 66 of at least 91%. Inan embodiment, the GH62 polypeptide has a sequence identity to SEQ IDNO: 66 of at least 92%. In an embodiment, the GH62 polypeptide has asequence identity to SEQ ID NO: 66 of at least 93%. In an embodiment,the GH62 polypeptide has a sequence identity to SEQ ID NO: 66 of atleast 94%. In an embodiment, the GH62 polypeptide has a sequenceidentity to SEQ ID NO: 66 of at least 95%. In an embodiment, the GH62polypeptide has a sequence identity to SEQ ID NO: 66 of at least 96%. Inan embodiment, the GH62 polypeptide has a sequence identity to SEQ IDNO: 66 of at least 97%. In an embodiment, the GH62 polypeptide has asequence identity to SEQ ID NO: 66 of at least 98%. In an embodiment,the GH62 polypeptide has a sequence identity to SEQ ID NO: 66 of atleast 99%.

In one embodiment, the polypeptide comprises one or more amino acidsubstitutions, and/or one or more amino acid deletions, and/or one ormore amino acid insertions or any combination thereof in between 1 and10 positions, such as 1, 2, 3, 4, 5, 6, 7, 8, 9 or 10 positions of SEQID NO: 66. In one embodiment, the polypeptide comprises one or moreamino acid substitutions, and/or one or more amino acid deletions,and/or one or more amino acid insertions or any combination thereof inbetween 1 and 10 positions, such as 1, 2, 3, 4, 5, 6, 7, 8, 9 or 10positions of SEQ ID NO: 69. In one embodiment, the polypeptidepreferably comprises or consists of the amino acid sequence of SEQ IDNO: 66 or an allelic variant thereof; comprises SEQ ID NO: 66 or anallelic variant thereof and a N-terminal and/or C-terminal His-tagand/or HQ-tag such as SEQ ID NO: 69; or is a fragment thereof havingarabinofuranosidase activity and having at least 90% of the length ofSEQ ID NO: 66. In another embodiment, the polypeptide comprises orconsists of amino acids 1 to 302 of SEQ ID NO: 66. In anotherembodiment, the polypeptide comprises or consists of amino acids 1 to311 of SEQ ID NO: 69. In an embodiment, the polypeptide has beenisolated.

In another embodiment, the composition comprises a GH62 polypeptidehaving arabinofuranosidase activity, wherein GH62 polypeptide havingarabinofuranosidase activity has a sequence identity to the maturepolypeptide of SEQ ID NO: 104 of at least 80%, e.g., at least 85%, atleast 86%, at least 87%, at least 88%, at least 89%, at least 90%, atleast 91%, at least 92%, at least 93%, at least 94%, at least 95%, atleast 96%, at least 97%, at least 98%, at least 99%, or 100%.

In one embodiment, the polypeptide comprises one or more amino acidsubstitutions, and/or one or more amino acid deletions, and/or one ormore amino acid insertions or any combination thereof in between 1 and10 positions, such as 1, 2, 3, 4, 5, 6, 7, 8, 9 or 10 positions of themature polypeptide of SEQ ID NO: 104. In one embodiment, the polypeptidepreferably comprises or consists of the amino acid sequence of SEQ IDNO: 104 or an allelic variant thereof; comprises the amino acid sequenceof SEQ ID NO: 104 and a N-terminal and/or C-terminal His-tag and/orHQ-tag; or is a fragment thereof having arabinofuranosidase activity andhaving at least 90% of the length of the mature polypeptide. In anotherembodiment, the polypeptide comprises or consists of the maturepolypeptide of SEQ ID NO: 104. In another embodiment, the polypeptidecomprises or consists of amino acids 1 to 302 of SEQ ID NO: 104. In anembodiment, the polypeptide has been isolated.

In an embodiment, the composition comprises a GH62 polypeptide havingarabinofuranosidase activity having a sequence identity to SEQ ID NO:105 of at least 80%. In an embodiment, the GH62 polypeptide has asequence identity to SEQ ID NO: 105 of at least 85%. In an embodiment,the GH62 polypeptide has a sequence identity to SEQ ID NO: 105 of atleast 86%. In an embodiment, the GH62 polypeptide has a sequenceidentity to SEQ ID NO: 105 of at least 87%. In an embodiment, the GH62polypeptide has a sequence identity to SEQ ID NO: 105 of at least 88%.In an embodiment, the GH62 polypeptide has a sequence identity to SEQ IDNO: 105 of at least 89%. In an embodiment, the GH62 polypeptide has asequence identity to SEQ ID NO: 105 of at least 90%. In an embodiment,the GH62 polypeptide has a sequence identity to SEQ ID NO: 105 of atleast 91%. In an embodiment, the GH62 polypeptide has a sequenceidentity to SEQ ID NO: 105 of at least 92%. In an embodiment, the GH62polypeptide has a sequence identity to SEQ ID NO: 105 of at least 93%.In an embodiment, the GH62 polypeptide has a sequence identity to SEQ IDNO: 105 of at least 94%. In an embodiment, the GH62 polypeptide has asequence identity to SEQ ID NO: 105 of at least 95%. In an embodiment,the GH62 polypeptide has a sequence identity to SEQ ID NO: 105 of atleast 96%. In an embodiment, the GH62 polypeptide has a sequenceidentity to SEQ ID NO: 105 of at least 97%. In an embodiment, the GH62polypeptide has a sequence identity to SEQ ID NO: 105 of at least 98%.In an embodiment, the GH62 polypeptide has a sequence identity to SEQ IDNO: 105 of at least 99%.

In one embodiment, the polypeptide comprises one or more amino acidsubstitutions, and/or one or more amino acid deletions, and/or one ormore amino acid insertions or any combination thereof in between 1 and10 positions, such as 1, 2, 3, 4, 5, 6, 7, 8, 9 or 10 positions of SEQID NO: 105. In one embodiment, the polypeptide preferably comprises orconsists of the amino acid sequence of SEQ ID NO: 105 or an allelicvariant thereof; comprises SEQ ID NO: 105 or an allelic variant thereofand a N-terminal and/or C-terminal His-tag and/or HQ-tag; or is afragment thereof having arabinofuranosidase activity and having at least90% of the length of SEQ ID NO: 105. In another embodiment, thepolypeptide comprises or consists of amino acids 1 to 302 of SEQ ID NO:105. In an embodiment, the polypeptide has been isolated.

In another embodiment, the composition comprises a GH62 polypeptidehaving arabinofuranosidase activity, wherein GH62 polypeptide havingarabinofuranosidase activity has a sequence identity to the maturepolypeptide of SEQ ID NO: 107 of at least 80%, e.g., at least 85%, atleast 86%, at least 87%, at least 88%, at least 89%, at least 90%, atleast 91%, at least 92%, at least 93%, at least 94%, at least 95%, atleast 96%, at least 97%, at least 98%, at least 99%, or 100%.

In one embodiment, the polypeptide comprises one or more amino acidsubstitutions, and/or one or more amino acid deletions, and/or one ormore amino acid insertions or any combination thereof in between 1 and10 positions, such as 1, 2, 3, 4, 5, 6, 7, 8, 9 or 10 positions of themature polypeptide of SEQ ID NO: 107. In one embodiment, the polypeptidepreferably comprises or consists of the amino acid sequence of SEQ IDNO: 107 or an allelic variant thereof; comprises the amino acid sequenceof SEQ ID NO: 107 and a N-terminal and/or C-terminal His-tag and/orHQ-tag such as the mature polypeptide of SEQ ID NO: 110 or SEQ ID NO:111; or is a fragment thereof having arabinofuranosidase activity andhaving at least 90% of the length of the mature polypeptide. In anotherembodiment, the polypeptide comprises or consists of the maturepolypeptide of SEQ ID NO: 107. In another embodiment, the polypeptidecomprises or consists of amino acids 1 to 464 of SEQ ID NO: 107. Inanother embodiment, the polypeptide comprises or consists of the maturepolypeptide of SEQ ID NO: 110. In another embodiment, the polypeptidecomprises or consists of amino acids 1 to 472 of SEQ ID NO: 110. In anembodiment, the polypeptide has been isolated.

In an embodiment, the composition comprises a GH62 polypeptide havingarabinofuranosidase activity having a sequence identity to SEQ ID NO:108 of at least 80%. In an embodiment, the GH62 polypeptide has asequence identity to SEQ ID NO: 108 of at least 85%. In an embodiment,the GH62 polypeptide has a sequence identity to SEQ ID NO: 108 of atleast 86%. In an embodiment, the GH62 polypeptide has a sequenceidentity to SEQ ID NO: 108 of at least 87%. In an embodiment, the GH62polypeptide has a sequence identity to SEQ ID NO: 108 of at least 88%.In an embodiment, the GH62 polypeptide has a sequence identity to SEQ IDNO: 108 of at least 89%. In an embodiment, the GH62 polypeptide has asequence identity to SEQ ID NO: 108 of at least 90%. In an embodiment,the GH62 polypeptide has a sequence identity to SEQ ID NO: 108 of atleast 91%. In an embodiment, the GH62 polypeptide has a sequenceidentity to SEQ ID NO: 108 of at least 92%. In an embodiment, the GH62polypeptide has a sequence identity to SEQ ID NO: 108 of at least 93%.In an embodiment, the GH62 polypeptide has a sequence identity to SEQ IDNO: 108 of at least 94%. In an embodiment, the GH62 polypeptide has asequence identity to SEQ ID NO: 108 of at least 95%. In an embodiment,the GH62 polypeptide has a sequence identity to SEQ ID NO: 108 of atleast 96%. In an embodiment, the GH62 polypeptide has a sequenceidentity to SEQ ID NO: 108 of at least 97%. In an embodiment, the GH62polypeptide has a sequence identity to SEQ ID NO: 108 of at least 98%.In an embodiment, the GH62 polypeptide has a sequence identity to SEQ IDNO: 108 of at least 99%.

In one embodiment, the polypeptide comprises one or more amino acidsubstitutions, and/or one or more amino acid deletions, and/or one ormore amino acid insertions or any combination thereof in between 1 and10 positions, such as 1, 2, 3, 4, 5, 6, 7, 8, 9 or 10 positions of SEQID NO: 108. In one embodiment, the polypeptide comprises one or moreamino acid substitutions, and/or one or more amino acid deletions,and/or one or more amino acid insertions or any combination thereof inbetween 1 and 10 positions, such as 1, 2, 3, 4, 5, 6, 7, 8, 9 or 10positions of SEQ ID NO: 111. In one embodiment, the polypeptidepreferably comprises or consists of the amino acid sequence of SEQ IDNO: 108 or an allelic variant thereof; comprises SEQ ID NO: 108 or anallelic variant thereof and a N-terminal and/or C-terminal His-tagand/or HQ-tag such as SEQ ID NO: 111; or is a fragment thereof havingarabinofuranosidase activity and having at least 90% of the length ofSEQ ID NO: 108. In another embodiment, the polypeptide comprises orconsists of amino acids 1 to 464 of SEQ ID NO: 108. In anotherembodiment, the polypeptide comprises or consists of amino acids 1 to472 of SEQ ID NO: 111. In an embodiment, the polypeptide has beenisolated.

In another embodiment, the composition comprises a GH62 polypeptidehaving arabinofuranosidase activity, wherein GH62 polypeptide havingarabinofuranosidase activity has a sequence identity to the maturepolypeptide of SEQ ID NO: 113 of at least 80%, e.g., at least 85%, atleast 86%, at least 87%, at least 88%, at least 89%, at least 90%, atleast 91%, at least 92%, at least 93%, at least 94%, at least 95%, atleast 96%, at least 97%, at least 98%, at least 99%, or 100%.

In one embodiment, the polypeptide comprises one or more amino acidsubstitutions, and/or one or more amino acid deletions, and/or one ormore amino acid insertions or any combination thereof in between 1 and10 positions, such as 1, 2, 3, 4, 5, 6, 7, 8, 9 or 10 positions of themature polypeptide of SEQ ID NO: 113. In one embodiment, the polypeptidepreferably comprises or consists of the amino acid sequence of SEQ IDNO: 113 or an allelic variant thereof; comprises the amino acid sequenceof SEQ ID NO: 113 and a N-terminal and/or C-terminal His-tag and/orHQ-tag such as the mature polypeptide of SEQ ID NO: 116 or SEQ ID NO:117; or is a fragment thereof having arabinofuranosidase activity andhaving at least 90% of the length of the mature polypeptide. In anotherembodiment, the polypeptide comprises or consists of the maturepolypeptide of SEQ ID NO: 113. In another embodiment, the polypeptidecomprises or consists of amino acids 1 to 364 of SEQ ID NO: 113. Inanother embodiment, the polypeptide comprises or consists of the maturepolypeptide of SEQ ID NO: 116. In another embodiment, the polypeptidecomprises or consists of amino acids 1 to 372 of SEQ ID NO: 116. In anembodiment, the polypeptide has been isolated.

In an embodiment, the composition comprises a GH62 polypeptide havingarabinofuranosidase activity having a sequence identity to SEQ ID NO:114 of at least 80%. In an embodiment, the GH62 polypeptide has asequence identity to SEQ ID NO: 114 of at least 85%. In an embodiment,the GH62 polypeptide has a sequence identity to SEQ ID NO: 114 of atleast 86%. In an embodiment, the GH62 polypeptide has a sequenceidentity to SEQ ID NO: 114 of at least 87%. In an embodiment, the GH62polypeptide has a sequence identity to SEQ ID NO: 114 of at least 88%.In an embodiment, the GH62 polypeptide has a sequence identity to SEQ IDNO: 114 of at least 89%. In an embodiment, the GH62 polypeptide has asequence identity to SEQ ID NO: 114 of at least 90%. In an embodiment,the GH62 polypeptide has a sequence identity to SEQ ID NO: 114 of atleast 91%. In an embodiment, the GH62 polypeptide has a sequenceidentity to SEQ ID NO: 114 of at least 92%. In an embodiment, the GH62polypeptide has a sequence identity to SEQ ID NO: 114 of at least 93%.In an embodiment, the GH62 polypeptide has a sequence identity to SEQ IDNO: 114 of at least 94%. In an embodiment, the GH62 polypeptide has asequence identity to SEQ ID NO: 114 of at least 95%. In an embodiment,the GH62 polypeptide has a sequence identity to SEQ ID NO: 114 of atleast 96%. In an embodiment, the GH62 polypeptide has a sequenceidentity to SEQ ID NO: 114 of at least 97%. In an embodiment, the GH62polypeptide has a sequence identity to SEQ ID NO:

114 of at least 98%. In an embodiment, the GH62 polypeptide has asequence identity to SEQ ID NO: 114 of at least 99%.

In one embodiment, the polypeptide comprises one or more amino acidsubstitutions, and/or one or more amino acid deletions, and/or one ormore amino acid insertions or any combination thereof in between 1 and10 positions, such as 1, 2, 3, 4, 5, 6, 7, 8, 9 or 10 positions of SEQID NO: 114. In one embodiment, the polypeptide comprises one or moreamino acid substitutions, and/or one or more amino acid deletions,and/or one or more amino acid insertions or any combination thereof inbetween 1 and 10 positions, such as 1, 2, 3, 4, 5, 6, 7, 8, 9 or 10positions of SEQ ID NO: 117. In one embodiment, the polypeptidepreferably comprises or consists of the amino acid sequence of SEQ IDNO: 114 or an allelic variant thereof; comprises SEQ ID NO: 114 or anallelic variant thereof and a N-terminal and/or C-terminal His-tagand/or HQ-tag such as SEQ ID NO: 117; or is a fragment thereof havingarabinofuranosidase activity and having at least 90% of the length ofSEQ ID NO: 114. In another embodiment, the polypeptide comprises orconsists of amino acids 1 to 364 of SEQ ID NO: 114. In anotherembodiment, the polypeptide comprises or consists of amino acids 1 to372 of SEQ ID NO: 117. In an embodiment, the polypeptide has beenisolated.

In another embodiment, the composition comprises a GH62 polypeptidehaving arabinofuranosidase activity, wherein GH62 polypeptide havingarabinofuranosidase activity has a sequence identity to the maturepolypeptide of SEQ ID NO: 119 of at least 80%, e.g., at least 85%, atleast 86%, at least 87%, at least 88%, at least 89%, at least 90%, atleast 91%, at least 92%, at least 93%, at least 94%, at least 95%, atleast 96%, at least 97%, at least 98%, at least 99%, or 100%.

In one embodiment, the polypeptide comprises one or more amino acidsubstitutions, and/or one or more amino acid deletions, and/or one ormore amino acid insertions or any combination thereof in between 1 and10 positions, such as 1, 2, 3, 4, 5, 6, 7, 8, 9 or 10 positions of themature polypeptide of SEQ ID NO: 119. In one embodiment, the polypeptidepreferably comprises or consists of the amino acid sequence of SEQ IDNO: 119 or an allelic variant thereof; comprises the amino acid sequenceof SEQ ID NO: 119 and a N-terminal and/or C-terminal His-tag and/orHQ-tag; or is a fragment thereof having arabinofuranosidase activity andhaving at least 90% of the length of the mature polypeptide. In anotherembodiment, the polypeptide comprises or consists of the maturepolypeptide of SEQ ID NO: 119. In another embodiment, the polypeptidecomprises or consists of amino acids 1 to 357 of SEQ ID NO: 119. In anembodiment, the polypeptide has been isolated.

In an embodiment, the composition comprises a GH62 polypeptide havingarabinofuranosidase activity having a sequence identity to SEQ ID NO:120 of at least 80%. In an embodiment, the GH62 polypeptide has asequence identity to SEQ ID NO: 120 of at least 85%. In an embodiment,the GH62 polypeptide has a sequence identity to SEQ ID NO: 120 of atleast 86%. In an embodiment, the GH62 polypeptide has a sequenceidentity to SEQ ID NO: 120 of at least 87%. In an embodiment, the GH62polypeptide has a sequence identity to SEQ ID NO: 120 of at least 88%.In an embodiment, the GH62 polypeptide has a sequence identity to SEQ IDNO: 120 of at least 89%. In an embodiment, the GH62 polypeptide has asequence identity to SEQ ID NO: 120 of at least 90%. In an embodiment,the GH62 polypeptide has a sequence identity to SEQ ID NO: 120 of atleast 91%. In an embodiment, the GH62 polypeptide has a sequenceidentity to SEQ ID NO: 120 of at least 92%. In an embodiment, the GH62polypeptide has a sequence identity to SEQ ID NO: 120 of at least 93%.In an embodiment, the GH62 polypeptide has a sequence identity to SEQ IDNO: 120 of at least 94%. In an embodiment, the GH62 polypeptide has asequence identity to SEQ ID NO: 120 of at least 95%. In an embodiment,the GH62 polypeptide has a sequence identity to SEQ ID NO: 120 of atleast 96%. In an embodiment, the GH62 polypeptide has a sequenceidentity to SEQ ID NO: 120 of at least 97%. In an embodiment, the GH62polypeptide has a sequence identity to SEQ ID NO: 120 of at least 98%.In an embodiment, the GH62 polypeptide has a sequence identity to SEQ IDNO: 120 of at least 99%.

In one embodiment, the polypeptide comprises one or more amino acidsubstitutions, and/or one or more amino acid deletions, and/or one ormore amino acid insertions or any combination thereof in between 1 and10 positions, such as 1, 2, 3, 4, 5, 6, 7, 8, 9 or 10 positions of SEQID NO: 120. In one embodiment, the polypeptide preferably comprises orconsists of the amino acid sequence of SEQ ID NO: 120 or an allelicvariant thereof; comprises SEQ ID NO: 120 or an allelic variant thereofand a N-terminal and/or C-terminal His-tag and/or HQ-tag; or is afragment thereof having arabinofuranosidase activity and having at least90% of the length of SEQ ID NO: 120. In another embodiment, thepolypeptide comprises or consists of amino acids 1 to 357 of SEQ ID NO:120. In an embodiment, the polypeptide has been isolated.

In another embodiment, the composition comprises a GH62 polypeptidehaving arabinofuranosidase activity, wherein GH62 polypeptide havingarabinofuranosidase activity has a sequence identity to the maturepolypeptide of SEQ ID NO: 122 of at least 80%, e.g., at least 85%, atleast 86%, at least 87%, at least 88%, at least 89%, at least 90%, atleast 91%, at least 92%, at least 93%, at least 94%, at least 95%, atleast 96%, at least 97%, at least 98%, at least 99%, or 100%.

In one embodiment, the polypeptide comprises one or more amino acidsubstitutions, and/or one or more amino acid deletions, and/or one ormore amino acid insertions or any combination thereof in between 1 and10 positions, such as 1, 2, 3, 4, 5, 6, 7, 8, 9 or 10 positions of themature polypeptide of SEQ ID NO: 122. In one embodiment, the polypeptidepreferably comprises or consists of the amino acid sequence of SEQ IDNO: 122 or an allelic variant thereof; comprises the amino acid sequenceof SEQ ID NO: 122 and a N-terminal and/or C-terminal His-tag and/orHQ-tag; or is a fragment thereof having arabinofuranosidase activity andhaving at least 90% of the length of the mature polypeptide. In anotherembodiment, the polypeptide comprises or consists of the maturepolypeptide of SEQ ID NO: 122. In another embodiment, the polypeptidecomprises or consists of amino acids 1 to 302 of SEQ ID NO: 122. In anembodiment, the polypeptide has been isolated.

In an embodiment, the composition comprises a GH62 polypeptide havingarabinofuranosidase activity having a sequence identity to SEQ ID NO:123 of at least 80%. In an embodiment, the GH62 polypeptide has asequence identity to SEQ ID NO: 123 of at least 85%. In an embodiment,the GH62 polypeptide has a sequence identity to SEQ ID NO: 123 of atleast 86%. In an embodiment, the GH62 polypeptide has a sequenceidentity to SEQ ID NO: 123 of at least 87%. In an embodiment, the GH62polypeptide has a sequence identity to SEQ ID NO: 123 of at least 88%.In an embodiment, the GH62 polypeptide has a sequence identity to SEQ IDNO: 123 of at least 89%. In an embodiment, the GH62 polypeptide has asequence identity to SEQ ID NO: 123 of at least 90%. In an embodiment,the GH62 polypeptide has a sequence identity to SEQ ID NO: 123 of atleast 91%. In an embodiment, the GH62 polypeptide has a sequenceidentity to SEQ ID NO: 123 of at least 92%. In an embodiment, the GH62polypeptide has a sequence identity to SEQ ID NO: 123 of at least 93%.In an embodiment, the GH62 polypeptide has a sequence identity to SEQ IDNO: 123 of at least 94%. In an embodiment, the GH62 polypeptide has asequence identity to SEQ ID NO: 123 of at least 95%. In an embodiment,the GH62 polypeptide has a sequence identity to SEQ ID NO: 123 of atleast 96%. In an embodiment, the GH62 polypeptide has a sequenceidentity to SEQ ID NO: 123 of at least 97%. In an embodiment, the GH62polypeptide has a sequence identity to SEQ ID NO: 123 of at least 98%.In an embodiment, the GH62 polypeptide has a sequence identity to SEQ IDNO: 123 of at least 99%.

In one embodiment, the polypeptide comprises one or more amino acidsubstitutions, and/or one or more amino acid deletions, and/or one ormore amino acid insertions or any combination thereof in between 1 and10 positions, such as 1, 2, 3, 4, 5, 6, 7, 8, 9 or 10 positions of SEQID NO: 123. In one embodiment, the polypeptide preferably comprises orconsists of the amino acid sequence of SEQ ID NO: 123 or an allelicvariant thereof; comprises SEQ ID NO: 123 or an allelic variant thereofand a N-terminal and/or C-terminal His-tag and/or HQ-tag; or is afragment thereof having arabinofuranosidase activity and having at least90% of the length of SEQ ID NO: 123. In another embodiment, thepolypeptide comprises or consists of amino acids 1 to 302 of SEQ ID NO:123. In an embodiment, the polypeptide has been isolated.

In another embodiment, the composition comprises a GH62 polypeptidehaving arabinofuranosidase activity, wherein GH62 polypeptide havingarabinofuranosidase activity has a sequence identity to the maturepolypeptide of SEQ ID NO: 125 of at least 80%, e.g., at least 85%, atleast 86%, at least 87%, at least 88%, at least 89%, at least 90%, atleast 91%, at least 92%, at least 93%, at least 94%, at least 95%, atleast 96%, at least 97%, at least 98%, at least 99%, or 100%.

In one embodiment, the polypeptide comprises one or more amino acidsubstitutions, and/or one or more amino acid deletions, and/or one ormore amino acid insertions or any combination thereof in between 1 and10 positions, such as 1, 2, 3, 4, 5, 6, 7, 8, 9 or 10 positions of themature polypeptide of SEQ ID NO: 125. In one embodiment, the polypeptidepreferably comprises or consists of the amino acid sequence of SEQ IDNO: 125 or an allelic variant thereof; comprises the amino acid sequenceof SEQ ID NO: 125 and a N-terminal and/or C-terminal His-tag and/orHQ-tag such as the mature polypeptide of SEQ ID NO: 128 or SEQ ID NO:129; or is a fragment thereof having arabinofuranosidase activity andhaving at least 90% of the length of the mature polypeptide. In anotherembodiment, the polypeptide comprises or consists of the maturepolypeptide of SEQ ID NO: 125. In another embodiment, the polypeptidecomprises or consists of amino acids 1 to 453 of SEQ ID NO: 125. Inanother embodiment, the polypeptide comprises or consists of the maturepolypeptide of SEQ ID NO: 128. In another embodiment, the polypeptidecomprises or consists of amino acids 1 to 461 of SEQ ID NO: 128. In anembodiment, the polypeptide has been isolated.

In an embodiment, the composition comprises a GH62 polypeptide havingarabinofuranosidase activity having a sequence identity to SEQ ID NO:126 of at least 80%. In an embodiment, the GH62 polypeptide has asequence identity to SEQ ID NO: 126 of at least 85%. In an embodiment,the GH62 polypeptide has a sequence identity to SEQ ID NO: 126 of atleast 86%. In an embodiment, the GH62 polypeptide has a sequenceidentity to SEQ ID NO: 126 of at least 87%. In an embodiment, the GH62polypeptide has a sequence identity to SEQ ID NO: 126 of at least 88%.In an embodiment, the GH62 polypeptide has a sequence identity to SEQ IDNO: 126 of at least 89%. In an embodiment, the GH62 polypeptide has asequence identity to SEQ ID NO: 126 of at least 90%. In an embodiment,the GH62 polypeptide has a sequence identity to SEQ ID NO: 126 of atleast 91%. In an embodiment, the GH62 polypeptide has a sequenceidentity to SEQ ID NO: 126 of at least 92%. In an embodiment, the GH62polypeptide has a sequence identity to SEQ ID NO: 126 of at least 93%.In an embodiment, the GH62 polypeptide has a sequence identity to SEQ IDNO: 126 of at least 94%. In an embodiment, the GH62 polypeptide has asequence identity to SEQ ID NO: 126 of at least 95%. In an embodiment,the GH62 polypeptide has a sequence identity to SEQ ID NO: 126 of atleast 96%. In an embodiment, the GH62 polypeptide has a sequenceidentity to SEQ ID NO: 126 of at least 97%. In an embodiment, the GH62polypeptide has a sequence identity to SEQ ID NO: 126 of at least 98%.In an embodiment, the GH62 polypeptide has a sequence identity to SEQ IDNO: 126 of at least 99%.

In one embodiment, the polypeptide comprises one or more amino acidsubstitutions, and/or one or more amino acid deletions, and/or one ormore amino acid insertions or any combination thereof in between 1 and10 positions, such as 1, 2, 3, 4, 5, 6, 7, 8, 9 or 10 positions of SEQID NO: 126. In one embodiment, the polypeptide comprises one or moreamino acid substitutions, and/or one or more amino acid deletions,and/or one or more amino acid insertions or any combination thereof inbetween 1 and 10 positions, such as 1, 2, 3, 4, 5, 6, 7, 8, 9 or 10positions of SEQ ID NO: 129. In one embodiment, the polypeptidepreferably comprises or consists of the amino acid sequence of SEQ IDNO: 126 or an allelic variant thereof; comprises SEQ ID NO: 126 or anallelic variant thereof and a N-terminal and/or C-terminal His-tagand/or HQ-tag such as SEQ ID NO: 129; or is a fragment thereof havingarabinofuranosidase activity and having at least 90% of the length ofSEQ ID NO: 126. In another embodiment, the polypeptide comprises orconsists of amino acids 1 to 453 of SEQ ID NO: 126. In anotherembodiment, the polypeptide comprises or consists of amino acids 1 to461 of SEQ ID NO: 129. In an embodiment, the polypeptide has beenisolated.

In another embodiment, the composition comprises a GH62 polypeptidehaving arabinofuranosidase activity, wherein GH62 polypeptide havingarabinofuranosidase activity has a sequence identity to the maturepolypeptide of SEQ ID NO: 131 of at least 80%, e.g., at least 85%, atleast 86%, at least 87%, at least 88%, at least 89%, at least 90%, atleast 91%, at least 92%, at least 93%, at least 94%, at least 95%, atleast 96%, at least 97%, at least 98%, at least 99%, or 100%.

In one embodiment, the polypeptide comprises one or more amino acidsubstitutions, and/or one or more amino acid deletions, and/or one ormore amino acid insertions or any combination thereof in between 1 and10 positions, such as 1, 2, 3, 4, 5, 6, 7, 8, 9 or 10 positions of themature polypeptide of SEQ ID NO: 131. In one embodiment, the polypeptidepreferably comprises or consists of the amino acid sequence of SEQ IDNO: 131 or an allelic variant thereof; comprises the amino acid sequenceof SEQ ID NO: 131 and a N-terminal and/or C-terminal His-tag and/orHQ-tag such as the mature polypeptide of SEQ ID NO: 134 or SEQ ID NO:135; or is a fragment thereof having arabinofuranosidase activity andhaving at least 90% of the length of the mature polypeptide. In anotherembodiment, the polypeptide comprises or consists of the maturepolypeptide of SEQ ID NO: 131. In another embodiment, the polypeptidecomprises or consists of amino acids 1 to 377 of SEQ ID NO: 131. Inanother embodiment, the polypeptide comprises or consists of the maturepolypeptide of SEQ ID NO: 134. In another embodiment, the polypeptidecomprises or consists of amino acids 1 to 385 of SEQ ID NO: 134. In anembodiment, the polypeptide has been isolated.

In an embodiment, the composition comprises a GH62 polypeptide havingarabinofuranosidase activity having a sequence identity to SEQ ID NO:132 of at least 80%. In an embodiment, the GH62 polypeptide has asequence identity to SEQ ID NO: 132 of at least 85%. In an embodiment,the GH62 polypeptide has a sequence identity to SEQ ID NO: 132 of atleast 86%. In an embodiment, the GH62 polypeptide has a sequenceidentity to SEQ ID NO: 132 of at least 87%. In an embodiment, the GH62polypeptide has a sequence identity to SEQ ID NO: 132 of at least 88%.In an embodiment, the GH62 polypeptide has a sequence identity to SEQ IDNO: 132 of at least 89%. In an embodiment, the GH62 polypeptide has asequence identity to SEQ ID NO: 132 of at least 90%. In an embodiment,the GH62 polypeptide has a sequence identity to SEQ ID NO: 132 of atleast 91%. In an embodiment, the GH62 polypeptide has a sequenceidentity to SEQ ID NO: 132 of at least 92%. In an embodiment, the GH62polypeptide has a sequence identity to SEQ ID NO: 132 of at least 93%.In an embodiment, the GH62 polypeptide has a sequence identity to SEQ IDNO: 132 of at least 94%. In an embodiment, the GH62 polypeptide has asequence identity to SEQ ID NO: 132 of at least 95%. In an embodiment,the GH62 polypeptide has a sequence identity to SEQ ID NO: 132 of atleast 96%. In an embodiment, the GH62 polypeptide has a sequenceidentity to SEQ ID NO: 132 of at least 97%. In an embodiment, the GH62polypeptide has a sequence identity to SEQ ID NO: 132 of at least 98%.In an embodiment, the GH62 polypeptide has a sequence identity to SEQ IDNO: 132 of at least 99%.

In one embodiment, the polypeptide comprises one or more amino acidsubstitutions, and/or one or more amino acid deletions, and/or one ormore amino acid insertions or any combination thereof in between 1 and10 positions, such as 1, 2, 3, 4, 5, 6, 7, 8, 9 or 10 positions of SEQID NO: 132. In one embodiment, the polypeptide comprises one or moreamino acid substitutions, and/or one or more amino acid deletions,and/or one or more amino acid insertions or any combination thereof inbetween 1 and 10 positions, such as 1, 2, 3, 4, 5, 6, 7, 8, 9 or 10positions of SEQ ID NO: 135. In one embodiment, the polypeptidepreferably comprises or consists of the amino acid sequence of SEQ IDNO: 132 or an allelic variant thereof; comprises SEQ ID NO: 132 or anallelic variant thereof and a N-terminal and/or C-terminal His-tagand/or HQ-tag such as SEQ ID NO: 135; or is a fragment thereof havingarabinofuranosidase activity and having at least 90% of the length ofSEQ ID NO: 132. In another embodiment, the polypeptide comprises orconsists of amino acids 1 to 377 of SEQ ID NO: 132. In anotherembodiment, the polypeptide comprises or consists of amino acids 1 to385 of SEQ ID NO: 135. In an embodiment, the polypeptide has beenisolated.

In another embodiment, the composition comprises a GH62 polypeptidehaving arabinofuranosidase activity, wherein GH62 polypeptide havingarabinofuranosidase activity has a sequence identity to the maturepolypeptide of SEQ ID NO: 137 of at least 80%, e.g., at least 85%, atleast 86%, at least 87%, at least 88%, at least 89%, at least 90%, atleast 91%, at least 92%, at least 93%, at least 94%, at least 95%, atleast 96%, at least 97%, at least 98%, at least 99%, or 100%.

In one embodiment, the polypeptide comprises one or more amino acidsubstitutions, and/or one or more amino acid deletions, and/or one ormore amino acid insertions or any combination thereof in between 1 and10 positions, such as 1, 2, 3, 4, 5, 6, 7, 8, 9 or 10 positions of themature polypeptide of SEQ ID NO: 137. In one embodiment, the polypeptidepreferably comprises or consists of the amino acid sequence of SEQ IDNO: 137 or an allelic variant thereof; comprises the amino acid sequenceof SEQ ID NO: 137 and a N-terminal and/or C-terminal His-tag and/orHQ-tag; or is a fragment thereof having arabinofuranosidase activity andhaving at least 90% of the length of the mature polypeptide. In anotherembodiment, the polypeptide comprises or consists of the maturepolypeptide of SEQ ID NO: 137. In another embodiment, the polypeptidecomprises or consists of amino acids 1 to 309 of SEQ ID NO: 137. In anembodiment, the polypeptide has been isolated.

In an embodiment, the composition comprises a GH62 polypeptide havingarabinofuranosidase activity having a sequence identity to SEQ ID NO:138 of at least 80%. In an embodiment, the GH62 polypeptide has asequence identity to SEQ ID NO: 138 of at least 85%. In an embodiment,the GH62 polypeptide has a sequence identity to SEQ ID NO: 138 of atleast 86%. In an embodiment, the GH62 polypeptide has a sequenceidentity to SEQ ID NO: 138 of at least 87%. In an embodiment, the GH62polypeptide has a sequence identity to SEQ ID NO: 138 of at least 88%.In an embodiment, the GH62 polypeptide has a sequence identity to SEQ IDNO: 138 of at least 89%. In an embodiment, the GH62 polypeptide has asequence identity to SEQ ID NO: 138 of at least 90%. In an embodiment,the GH62 polypeptide has a sequence identity to SEQ ID NO: 138 of atleast 91%. In an embodiment, the GH62 polypeptide has a sequenceidentity to SEQ ID NO: 138 of at least 92%. In an embodiment, the GH62polypeptide has a sequence identity to SEQ ID NO: 138 of at least 93%.In an embodiment, the GH62 polypeptide has a sequence identity to SEQ IDNO: 138 of at least 94%. In an embodiment, the GH62 polypeptide has asequence identity to SEQ ID NO: 138 of at least 95%. In an embodiment,the GH62 polypeptide has a sequence identity to SEQ ID NO: 138 of atleast 96%. In an embodiment, the GH62 polypeptide has a sequenceidentity to SEQ ID NO: 138 of at least 97%. In an embodiment, the GH62polypeptide has a sequence identity to SEQ ID NO: 138 of at least 98%.In an embodiment, the GH62 polypeptide has a sequence identity to SEQ IDNO: 138 of at least 99%.

In one embodiment, the polypeptide comprises one or more amino acidsubstitutions, and/or one or more amino acid deletions, and/or one ormore amino acid insertions or any combination thereof in between 1 and10 positions, such as 1, 2, 3, 4, 5, 6, 7, 8, 9 or 10 positions of SEQID NO: 138. In one embodiment, the polypeptide preferably comprises orconsists of the amino acid sequence of SEQ ID NO: 138 or an allelicvariant thereof; comprises SEQ ID NO: 138 or an allelic variant thereofand a N-terminal and/or C-terminal His-tag and/or HQ-tag; or is afragment thereof having arabinofuranosidase activity and having at least90% of the length of SEQ ID NO: 138. In another embodiment, thepolypeptide comprises or consists of amino acids 1 to 308 of SEQ ID NO:138. In an embodiment, the polypeptide has been isolated.

In another embodiment, the composition comprises a GH62 polypeptidehaving arabinofuranosidase activity, wherein GH62 polypeptide havingarabinofuranosidase activity has a sequence identity to the maturepolypeptide of SEQ ID NO: 140 of at least 80%, e.g., at least 85%, atleast 86%, at least 87%, at least 88%, at least 89%, at least 90%, atleast 91%, at least 92%, at least 93%, at least 94%, at least 95%, atleast 96%, at least 97%, at least 98%, at least 99%, or 100%.

In one embodiment, the polypeptide comprises one or more amino acidsubstitutions, and/or one or more amino acid deletions, and/or one ormore amino acid insertions or any combination thereof in between 1 and10 positions, such as 1, 2, 3, 4, 5, 6, 7, 8, 9 or 10 positions of themature polypeptide of SEQ ID NO: 140. In one embodiment, the polypeptidepreferably comprises or consists of the amino acid sequence of SEQ IDNO: 140 or an allelic variant thereof; comprises the amino acid sequenceof SEQ ID NO: 140 and a N-terminal and/or C-terminal His-tag and/orHQ-tag such as the mature polypeptide of SEQ ID NO: 143 or SEQ ID NO:144; or is a fragment thereof having arabinofuranosidase activity andhaving at least 90% of the length of the mature polypeptide. In anotherembodiment, the polypeptide comprises or consists of the maturepolypeptide of SEQ ID NO: 140. In another embodiment, the polypeptidecomprises or consists of amino acids 1 to 304 of SEQ ID NO: 140. Inanother embodiment, the polypeptide comprises or consists of the maturepolypeptide of SEQ ID NO: 143. In another embodiment, the polypeptidecomprises or consists of amino acids 1 to 312 of SEQ ID NO: 143. In anembodiment, the polypeptide has been isolated.

In an embodiment, the composition comprises a GH62 polypeptide havingarabinofuranosidase activity having a sequence identity to SEQ ID NO:141 of at least 80%. In an embodiment, the GH62 polypeptide has asequence identity to SEQ ID NO: 141 of at least 85%. In an embodiment,the GH62 polypeptide has a sequence identity to SEQ ID NO: 141 of atleast 86%. In an embodiment, the GH62 polypeptide has a sequenceidentity to SEQ ID NO: 141 of at least 87%. In an embodiment, the GH62polypeptide has a sequence identity to SEQ ID NO: 141 of at least 88%.In an embodiment, the GH62 polypeptide has a sequence identity to SEQ IDNO: 141 of at least 89%. In an embodiment, the GH62 polypeptide has asequence identity to SEQ ID NO: 141 of at least 90%. In an embodiment,the GH62 polypeptide has a sequence identity to SEQ ID NO: 141 of atleast 91%. In an embodiment, the GH62 polypeptide has a sequenceidentity to SEQ ID NO: 141 of at least 92%. In an embodiment, the GH62polypeptide has a sequence identity to SEQ ID NO: 141 of at least 93%.In an embodiment, the GH62 polypeptide has a sequence identity to SEQ IDNO: 141 of at least 94%. In an embodiment, the GH62 polypeptide has asequence identity to SEQ ID NO: 141 of at least 95%. In an embodiment,the GH62 polypeptide has a sequence identity to SEQ ID NO: 141 of atleast 96%. In an embodiment, the GH62 polypeptide has a sequenceidentity to SEQ ID NO: 141 of at least 97%. In an embodiment, the GH62polypeptide has a sequence identity to SEQ ID NO: 141 of at least 98%.In an embodiment, the GH62 polypeptide has a sequence identity to SEQ IDNO: 141 of at least 99%.

In one embodiment, the polypeptide comprises one or more amino acidsubstitutions, and/or one or more amino acid deletions, and/or one ormore amino acid insertions or any combination thereof in between 1 and10 positions, such as 1, 2, 3, 4, 5, 6, 7, 8, 9 or 10 positions of SEQID NO: 141. In one embodiment, the polypeptide comprises one or moreamino acid substitutions, and/or one or more amino acid deletions,and/or one or more amino acid insertions or any combination thereof inbetween 1 and 10 positions, such as 1, 2, 3, 4, 5, 6, 7, 8, 9 or 10positions of SEQ ID NO: 144. In one embodiment, the polypeptidepreferably comprises or consists of the amino acid sequence of SEQ IDNO: 141 or an allelic variant thereof; comprises SEQ ID NO: 141 or anallelic variant thereof and a N-terminal and/or C-terminal His-tagand/or HQ-tag such as SEQ ID NO: 144; or is a fragment thereof havingarabinofuranosidase activity and having at least 90% of the length ofSEQ ID NO: 141. In another embodiment, the polypeptide comprises orconsists of amino acids 1 to 304 of SEQ ID NO: 141. In anotherembodiment, the polypeptide comprises or consists of amino acids 1 to312 of SEQ ID NO: 144. In an embodiment, the polypeptide has beenisolated.

In another embodiment, the composition comprises a GH62 polypeptidehaving arabinofuranosidase activity, wherein GH62 polypeptide havingarabinofuranosidase activity has a sequence identity to the maturepolypeptide of SEQ ID NO: 146 of at least 80%, e.g., at least 85%, atleast 86%, at least 87%, at least 88%, at least 89%, at least 90%, atleast 91%, at least 92%, at least 93%, at least 94%, at least 95%, atleast 96%, at least 97%, at least 98%, at least 99%, or 100%.

In one embodiment, the polypeptide comprises one or more amino acidsubstitutions, and/or one or more amino acid deletions, and/or one ormore amino acid insertions or any combination thereof in between 1 and10 positions, such as 1, 2, 3, 4, 5, 6, 7, 8, 9 or 10 positions of themature polypeptide of SEQ ID NO: 146. In one embodiment, the polypeptidepreferably comprises or consists of the amino acid sequence of SEQ IDNO: 146 or an allelic variant thereof; comprises the amino acid sequenceof SEQ ID NO: 146 and a N-terminal and/or C-terminal His-tag and/orHQ-tag; or is a fragment thereof having arabinofuranosidase activity andhaving at least 90% of the length of the mature polypeptide. In anotherembodiment, the polypeptide comprises or consists of the maturepolypeptide of SEQ ID NO: 146. In another embodiment, the polypeptidecomprises or consists of amino acids 1 to 302 of SEQ ID NO: 146. In anembodiment, the polypeptide has been isolated.

In an embodiment, the composition comprises a GH62 polypeptide havingarabinofuranosidase activity having a sequence identity to SEQ ID NO:147 of at least 80%. In an embodiment, the GH62 polypeptide has asequence identity to SEQ ID NO: 147 of at least 85%. In an embodiment,the GH62 polypeptide has a sequence identity to SEQ ID NO: 147 of atleast 86%. In an embodiment, the GH62 polypeptide has a sequenceidentity to SEQ ID NO: 147 of at least 87%. In an embodiment, the GH62polypeptide has a sequence identity to SEQ ID NO: 147 of at least 88%.In an embodiment, the GH62 polypeptide has a sequence identity to SEQ IDNO: 147 of at least 89%. In an embodiment, the GH62 polypeptide has asequence identity to SEQ ID NO: 147 of at least 90%. In an embodiment,the GH62 polypeptide has a sequence identity to SEQ ID NO: 147 of atleast 91%. In an embodiment, the GH62 polypeptide has a sequenceidentity to SEQ ID NO: 147 of at least 92%. In an embodiment, the GH62polypeptide has a sequence identity to SEQ ID NO: 147 of at least 93%.In an embodiment, the GH62 polypeptide has a sequence identity to SEQ IDNO: 147 of at least 94%. In an embodiment, the GH62 polypeptide has asequence identity to SEQ ID NO: 147 of at least 95%. In an embodiment,the GH62 polypeptide has a sequence identity to SEQ ID NO: 147 of atleast 96%. In an embodiment, the GH62 polypeptide has a sequenceidentity to SEQ ID NO: 147 of at least 97%. In an embodiment, the GH62polypeptide has a sequence identity to SEQ ID NO: 147 of at least 98%.In an embodiment, the GH62 polypeptide has a sequence identity to SEQ IDNO: 147 of at least 99%.

In one embodiment, the polypeptide comprises one or more amino acidsubstitutions, and/or one or more amino acid deletions, and/or one ormore amino acid insertions or any combination thereof in between 1 and10 positions, such as 1, 2, 3, 4, 5, 6, 7, 8, 9 or 10 positions of SEQID NO: 147. In one embodiment, the polypeptide preferably comprises orconsists of the amino acid sequence of SEQ ID NO: 147 or an allelicvariant thereof; comprises SEQ ID NO: 147 or an allelic variant thereofand a N-terminal and/or C-terminal His-tag and/or HQ-tag; or is afragment thereof having arabinofuranosidase activity and having at least90% of the length of SEQ ID NO: 147. In another embodiment, thepolypeptide comprises or consists of amino acids 1 to 302 of SEQ ID NO:147. In an embodiment, the polypeptide has been isolated.

In another embodiment, the composition comprises a GH62 polypeptidehaving arabinofuranosidase activity, wherein GH62 polypeptide havingarabinofuranosidase activity has a sequence identity to the maturepolypeptide of SEQ ID NO: 149 of at least 80%, e.g., at least 85%, atleast 86%, at least 87%, at least 88%, at least 89%, at least 90%, atleast 91%, at least 92%, at least 93%, at least 94%, at least 95%, atleast 96%, at least 97%, at least 98%, at least 99%, or 100%.

In one embodiment, the polypeptide comprises one or more amino acidsubstitutions, and/or one or more amino acid deletions, and/or one ormore amino acid insertions or any combination thereof in between 1 and10 positions, such as 1, 2, 3, 4, 5, 6, 7, 8, 9 or 10 positions of themature polypeptide of SEQ ID NO: 149. In one embodiment, the polypeptidepreferably comprises or consists of the amino acid sequence of SEQ IDNO: 149 or an allelic variant thereof; comprises the amino acid sequenceof SEQ ID NO: 149 and a N-terminal and/or C-terminal His-tag and/orHQ-tag such as the mature polypeptide of SEQ ID NO: 152 or SEQ ID NO:153; or is a fragment thereof having arabinofuranosidase activity andhaving at least 90% of the length of the mature polypeptide. In anotherembodiment, the polypeptide comprises or consists of the maturepolypeptide of SEQ ID NO: 149. In another embodiment, the polypeptidecomprises or consists of amino acids 1 to 302 of SEQ ID NO: 149. Inanother embodiment, the polypeptide comprises or consists of the maturepolypeptide of SEQ ID NO: 152. In another embodiment, the polypeptidecomprises or consists of amino acids 1 to 310 of SEQ ID NO: 152. In anembodiment, the polypeptide has been isolated.

In an embodiment, the composition comprises a GH62 polypeptide havingarabinofuranosidase activity having a sequence identity to SEQ ID NO:150 of at least 80%. In an embodiment, the GH62 polypeptide has asequence identity to SEQ ID NO: 150 of at least 85%. In an embodiment,the GH62 polypeptide has a sequence identity to SEQ ID NO: 150 of atleast 86%. In an embodiment, the GH62 polypeptide has a sequenceidentity to SEQ ID NO: 150 of at least 87%. In an embodiment, the GH62polypeptide has a sequence identity to SEQ ID NO: 150 of at least 88%.In an embodiment, the GH62 polypeptide has a sequence identity to SEQ IDNO: 150 of at least 89%. In an embodiment, the GH62 polypeptide has asequence identity to SEQ ID NO: 150 of at least 90%. In an embodiment,the GH62 polypeptide has a sequence identity to SEQ ID NO: 150 of atleast 91%. In an embodiment, the GH62 polypeptide has a sequenceidentity to SEQ ID NO: 150 of at least 92%. In an embodiment, the GH62polypeptide has a sequence identity to SEQ ID NO: 150 of at least 93%.In an embodiment, the GH62 polypeptide has a sequence identity to SEQ IDNO: 150 of at least 94%. In an embodiment, the GH62 polypeptide has asequence identity to SEQ ID NO: 150 of at least 95%. In an embodiment,the GH62 polypeptide has a sequence identity to SEQ ID NO: 150 of atleast 96%. In an embodiment, the GH62 polypeptide has a sequenceidentity to SEQ ID NO: 150 of at least 97%. In an embodiment, the GH62polypeptide has a sequence identity to SEQ ID NO: 150 of at least 98%.In an embodiment, the GH62 polypeptide has a sequence identity to SEQ IDNO: 150 of at least 99%.

In one embodiment, the polypeptide comprises one or more amino acidsubstitutions, and/or one or more amino acid deletions, and/or one ormore amino acid insertions or any combination thereof in between 1 and10 positions, such as 1, 2, 3, 4, 5, 6, 7, 8, 9 or 10 positions of SEQID NO: 150. In one embodiment, the polypeptide comprises one or moreamino acid substitutions, and/or one or more amino acid deletions,and/or one or more amino acid insertions or any combination thereof inbetween 1 and 10 positions, such as 1, 2, 3, 4, 5, 6, 7, 8, 9 or 10positions of SEQ ID NO: 153. In one embodiment, the polypeptidepreferably comprises or consists of the amino acid sequence of SEQ IDNO: 150 or an allelic variant thereof; comprises SEQ ID NO: 150 or anallelic variant thereof and a N-terminal and/or C-terminal His-tagand/or HQ-tag such as SEQ ID NO: 153; or is a fragment thereof havingarabinofuranosidase activity and having at least 90% of the length ofSEQ ID NO: 150. In another embodiment, the polypeptide comprises orconsists of amino acids 1 to 302 of SEQ ID NO: 150. In anotherembodiment, the polypeptide comprises or consists of amino acids 1 to310 of SEQ ID NO: 153. In an embodiment, the polypeptide has beenisolated.

In another embodiment, the composition comprises a GH62 polypeptidehaving arabinofuranosidase activity, wherein GH62 polypeptide havingarabinofuranosidase activity has a sequence identity to the maturepolypeptide of SEQ ID NO: 155 of at least 80%, e.g., at least 85%, atleast 86%, at least 87%, at least 88%, at least 89%, at least 90%, atleast 91%, at least 92%, at least 93%, at least 94%, at least 95%, atleast 96%, at least 97%, at least 98%, at least 99%, or 100%.

In one embodiment, the polypeptide comprises one or more amino acidsubstitutions, and/or one or more amino acid deletions, and/or one ormore amino acid insertions or any combination thereof in between 1 and10 positions, such as 1, 2, 3, 4, 5, 6, 7, 8, 9 or 10 positions of themature polypeptide of SEQ ID NO: 155. In one embodiment, the polypeptidepreferably comprises or consists of the amino acid sequence of SEQ IDNO: 155 or an allelic variant thereof; comprises the amino acid sequenceof SEQ ID NO: 155 and a N-terminal and/or C-terminal His-tag and/orHQ-tag; or is a fragment thereof having arabinofuranosidase activity andhaving at least 90% of the length of the mature polypeptide. In anotherembodiment, the polypeptide comprises or consists of the maturepolypeptide of SEQ ID NO: 155. In another embodiment, the polypeptidecomprises or consists of amino acids 1 to 316 of SEQ ID NO: 155. In anembodiment, the polypeptide has been isolated.

In an embodiment, the composition comprises a GH62 polypeptide havingarabinofuranosidase activity having a sequence identity to SEQ ID NO:156 of at least 80%. In an embodiment, the GH62 polypeptide has asequence identity to SEQ ID NO: 156 of at least 85%. In an embodiment,the GH62 polypeptide has a sequence identity to SEQ ID NO: 156 of atleast 86%. In an embodiment, the GH62 polypeptide has a sequenceidentity to SEQ ID NO: 156 of at least 87%. In an embodiment, the GH62polypeptide has a sequence identity to SEQ ID NO: 156 of at least 88%.In an embodiment, the GH62 polypeptide has a sequence identity to SEQ IDNO: 156 of at least 89%. In an embodiment, the GH62 polypeptide has asequence identity to SEQ ID NO: 156 of at least 90%. In an embodiment,the GH62 polypeptide has a sequence identity to SEQ ID NO: 156 of atleast 91%. In an embodiment, the GH62 polypeptide has a sequenceidentity to SEQ ID NO: 156 of at least 92%. In an embodiment, the GH62polypeptide has a sequence identity to SEQ ID NO: 156 of at least 93%.In an embodiment, the GH62 polypeptide has a sequence identity to SEQ IDNO: 156 of at least 94%. In an embodiment, the GH62 polypeptide has asequence identity to SEQ ID NO: 156 of at least 95%. In an embodiment,the GH62 polypeptide has a sequence identity to SEQ ID NO: 156 of atleast 96%. In an embodiment, the GH62 polypeptide has a sequenceidentity to SEQ ID NO: 156 of at least 97%. In an embodiment, the GH62polypeptide has a sequence identity to SEQ ID NO: 156 of at least 98%.In an embodiment, the GH62 polypeptide has a sequence identity to SEQ IDNO: 156 of at least 99%.

In one embodiment, the polypeptide comprises one or more amino acidsubstitutions, and/or one or more amino acid deletions, and/or one ormore amino acid insertions or any combination thereof in between 1 and10 positions, such as 1, 2, 3, 4, 5, 6, 7, 8, 9 or 10 positions of SEQID NO: 156. In one embodiment, the polypeptide preferably comprises orconsists of the amino acid sequence of SEQ ID NO: 156 or an allelicvariant thereof; comprises SEQ ID NO: 156 or an allelic variant thereofand a N-terminal and/or C-terminal His-tag and/or HQ-tag; or is afragment thereof having arabinofuranosidase activity and having at least90% of the length of SEQ ID NO: 156. In another embodiment, thepolypeptide comprises or consists of amino acids 1 to 316 of SEQ ID NO:156. In an embodiment, the polypeptide has been isolated.

In another embodiment, the composition comprises a GH62 polypeptidehaving arabinofuranosidase activity, wherein GH62 polypeptide havingarabinofuranosidase activity has a sequence identity to the maturepolypeptide of SEQ ID NO: 158 of at least 80%, e.g., at least 85%, atleast 86%, at least 87%, at least 88%, at least 89%, at least 90%, atleast 91%, at least 92%, at least 93%, at least 94%, at least 95%, atleast 96%, at least 97%, at least 98%, at least 99%, or 100%.

In one embodiment, the polypeptide comprises one or more amino acidsubstitutions, and/or one or more amino acid deletions, and/or one ormore amino acid insertions or any combination thereof in between 1 and10 positions, such as 1, 2, 3, 4, 5, 6, 7, 8, 9 or 10 positions of themature polypeptide of SEQ ID NO: 158. In one embodiment, the polypeptidepreferably comprises or consists of the amino acid sequence of SEQ IDNO: 158 or an allelic variant thereof; comprises the amino acid sequenceof SEQ ID NO: 158 and a N-terminal and/or C-terminal His-tag and/orHQ-tag; or is a fragment thereof having arabinofuranosidase activity andhaving at least 90% of the length of the mature polypeptide. In anotherembodiment, the polypeptide comprises or consists of the maturepolypeptide of SEQ ID NO: 158. In another embodiment, the polypeptidecomprises or consists of amino acids 1 to 316 of SEQ ID NO: 158. In anembodiment, the polypeptide has been isolated.

In an embodiment, the composition comprises a GH62 polypeptide havingarabinofuranosidase activity having a sequence identity to SEQ ID NO:159 of at least 80%. In an embodiment, the GH62 polypeptide has asequence identity to SEQ ID NO: 159 of at least 85%. In an embodiment,the GH62 polypeptide has a sequence identity to SEQ ID NO: 159 of atleast 86%. In an embodiment, the GH62 polypeptide has a sequenceidentity to SEQ ID NO: 159 of at least 87%. In an embodiment, the GH62polypeptide has a sequence identity to SEQ ID NO: 159 of at least 88%.In an embodiment, the GH62 polypeptide has a sequence identity to SEQ IDNO: 159 of at least 89%. In an embodiment, the GH62 polypeptide has asequence identity to SEQ ID NO: 159 of at least 90%. In an embodiment,the GH62 polypeptide has a sequence identity to SEQ ID NO: 159 of atleast 91%. In an embodiment, the GH62 polypeptide has a sequenceidentity to SEQ ID NO: 159 of at least 92%. In an embodiment, the GH62polypeptide has a sequence identity to SEQ ID NO: 159 of at least 93%.In an embodiment, the GH62 polypeptide has a sequence identity to SEQ IDNO: 159 of at least 94%. In an embodiment, the GH62 polypeptide has asequence identity to SEQ ID NO: 159 of at least 95%. In an embodiment,the GH62 polypeptide has a sequence identity to SEQ ID NO: 159 of atleast 96%. In an embodiment, the GH62 polypeptide has a sequenceidentity to SEQ ID NO: 159 of at least 97%. In an embodiment, the GH62polypeptide has a sequence identity to SEQ ID NO: 159 of at least 98%.In an embodiment, the GH62 polypeptide has a sequence identity to SEQ IDNO: 159 of at least 99%.

In one embodiment, the polypeptide comprises one or more amino acidsubstitutions, and/or one or more amino acid deletions, and/or one ormore amino acid insertions or any combination thereof in between 1 and10 positions, such as 1, 2, 3, 4, 5, 6, 7, 8, 9 or 10 positions of SEQID NO: 159. In one embodiment, the polypeptide preferably comprises orconsists of the amino acid sequence of SEQ ID NO: 159 or an allelicvariant thereof; comprises SEQ ID NO: 159 or an allelic variant thereofand a N-terminal and/or C-terminal His-tag and/or HQ-tag; or is afragment thereof having arabinofuranosidase activity and having at least90% of the length of SEQ ID NO: 159. In another embodiment, thepolypeptide comprises or consists of amino acids 1 to 316 of SEQ ID NO:159. In an embodiment, the polypeptide has been isolated.

In another embodiment, the composition comprises a GH62 polypeptidehaving arabinofuranosidase activity, wherein GH62 polypeptide havingarabinofuranosidase activity has a sequence identity to the maturepolypeptide of SEQ ID NO: 161 of at least 80%, e.g., at least 85%, atleast 86%, at least 87%, at least 88%, at least 89%, at least 90%, atleast 91%, at least 92%, at least 93%, at least 94%, at least 95%, atleast 96%, at least 97%, at least 98%, at least 99%, or 100%.

In one embodiment, the polypeptide comprises one or more amino acidsubstitutions, and/or one or more amino acid deletions, and/or one ormore amino acid insertions or any combination thereof in between 1 and10 positions, such as 1, 2, 3, 4, 5, 6, 7, 8, 9 or 10 positions of themature polypeptide of SEQ ID NO: 161. In one embodiment, the polypeptidepreferably comprises or consists of the amino acid sequence of SEQ IDNO: 161 or an allelic variant thereof; comprises the amino acid sequenceof SEQ ID NO: 161 and a N-terminal and/or C-terminal His-tag and/orHQ-tag; or is a fragment thereof having arabinofuranosidase activity andhaving at least 90% of the length of the mature polypeptide. In anotherembodiment, the polypeptide comprises or consists of the maturepolypeptide of SEQ ID NO: 161. In another embodiment, the polypeptidecomprises or consists of amino acids 1 to 303 of SEQ ID NO: 161. In anembodiment, the polypeptide has been isolated.

In an embodiment, the composition comprises a GH62 polypeptide havingarabinofuranosidase activity having a sequence identity to SEQ ID NO:162 of at least 80%. In an embodiment, the GH62 polypeptide has asequence identity to SEQ ID NO: 162 of at least 85%. In an embodiment,the GH62 polypeptide has a sequence identity to SEQ ID NO: 162 of atleast 86%. In an embodiment, the GH62 polypeptide has a sequenceidentity to SEQ ID NO: 162 of at least 87%. In an embodiment, the GH62polypeptide has a sequence identity to SEQ ID NO: 162 of at least 88%.In an embodiment, the GH62 polypeptide has a sequence identity to SEQ IDNO: 162 of at least 89%. In an embodiment, the GH62 polypeptide has asequence identity to SEQ ID NO: 162 of at least 90%. In an embodiment,the GH62 polypeptide has a sequence identity to SEQ ID NO: 162 of atleast 91%. In an embodiment, the GH62 polypeptide has a sequenceidentity to SEQ ID NO: 162 of at least 92%. In an embodiment, the GH62polypeptide has a sequence identity to SEQ ID NO: 162 of at least 93%.In an embodiment, the GH62 polypeptide has a sequence identity to SEQ IDNO: 162 of at least 94%. In an embodiment, the GH62 polypeptide has asequence identity to SEQ ID NO: 162 of at least 95%. In an embodiment,the GH62 polypeptide has a sequence identity to SEQ ID NO: 162 of atleast 96%. In an embodiment, the GH62 polypeptide has a sequenceidentity to SEQ ID NO: 162 of at least 97%. In an embodiment, the GH62polypeptide has a sequence identity to SEQ ID NO: 162 of at least 98%.In an embodiment, the GH62 polypeptide has a sequence identity to SEQ IDNO: 162 of at least 99%.

In one embodiment, the polypeptide comprises one or more amino acidsubstitutions, and/or one or more amino acid deletions, and/or one ormore amino acid insertions or any combination thereof in between 1 and10 positions, such as 1, 2, 3, 4, 5, 6, 7, 8, 9 or 10 positions of SEQID NO: 162. In one embodiment, the polypeptide preferably comprises orconsists of the amino acid sequence of SEQ ID NO: 162 or an allelicvariant thereof; comprises SEQ ID NO: 162 or an allelic variant thereofand a N-terminal and/or C-terminal His-tag and/or HQ-tag; or is afragment thereof having arabinofuranosidase activity and having at least90% of the length of SEQ ID NO: 162. In another embodiment, thepolypeptide comprises or consists of amino acids 1 to 303 of SEQ ID NO:162. In an embodiment, the polypeptide has been isolated.

In another embodiment, the composition comprises a GH62 polypeptidehaving arabinofuranosidase activity, wherein GH62 polypeptide havingarabinofuranosidase activity has a sequence identity to the maturepolypeptide of SEQ ID NO: 164 of at least 80%, e.g., at least 85%, atleast 86%, at least 87%, at least 88%, at least 89%, at least 90%, atleast 91%, at least 92%, at least 93%, at least 94%, at least 95%, atleast 96%, at least 97%, at least 98%, at least 99%, or 100%.

In one embodiment, the polypeptide comprises one or more amino acidsubstitutions, and/or one or more amino acid deletions, and/or one ormore amino acid insertions or any combination thereof in between 1 and10 positions, such as 1, 2, 3, 4, 5, 6, 7, 8, 9 or 10 positions of themature polypeptide of SEQ ID NO: 164. In one embodiment, the polypeptidepreferably comprises or consists of the amino acid sequence of SEQ IDNO: 164 or an allelic variant thereof; comprises the amino acid sequenceof SEQ ID NO: 164 and a N-terminal and/or C-terminal His-tag and/orHQ-tag; or is a fragment thereof having arabinofuranosidase activity andhaving at least 90% of the length of the mature polypeptide. In anotherembodiment, the polypeptide comprises or consists of the maturepolypeptide of SEQ ID NO: 164. In another embodiment, the polypeptidecomprises or consists of amino acids 1 to 361 of SEQ ID NO: 164. In anembodiment, the polypeptide has been isolated.

In an embodiment, the composition comprises a GH62 polypeptide havingarabinofuranosidase activity having a sequence identity to SEQ ID NO:165 of at least 80%. In an embodiment, the GH62 polypeptide has asequence identity to SEQ ID NO: 165 of at least 85%. In an embodiment,the GH62 polypeptide has a sequence identity to SEQ ID NO: 165 of atleast 86%. In an embodiment, the GH62 polypeptide has a sequenceidentity to SEQ ID NO: 165 of at least 87%. In an embodiment, the GH62polypeptide has a sequence identity to SEQ ID NO: 165 of at least 88%.In an embodiment, the GH62 polypeptide has a sequence identity to SEQ IDNO: 165 of at least 89%. In an embodiment, the GH62 polypeptide has asequence identity to SEQ ID NO: 165 of at least 90%. In an embodiment,the GH62 polypeptide has a sequence identity to SEQ ID NO: 165 of atleast 91%. In an embodiment, the GH62 polypeptide has a sequenceidentity to SEQ ID NO: 165 of at least 92%. In an embodiment, the GH62polypeptide has a sequence identity to SEQ ID NO: 165 of at least 93%.In an embodiment, the GH62 polypeptide has a sequence identity to SEQ IDNO: 165 of at least 94%. In an embodiment, the GH62 polypeptide has asequence identity to SEQ ID NO: 165 of at least 95%. In an embodiment,the GH62 polypeptide has a sequence identity to SEQ ID NO: 165 of atleast 96%. In an embodiment, the GH62 polypeptide has a sequenceidentity to SEQ ID NO: 165 of at least 97%. In an embodiment, the GH62polypeptide has a sequence identity to SEQ ID NO: 165 of at least 98%.In an embodiment, the GH62 polypeptide has a sequence identity to SEQ IDNO: 165 of at least 99%.

In one embodiment, the polypeptide comprises one or more amino acidsubstitutions, and/or one or more amino acid deletions, and/or one ormore amino acid insertions or any combination thereof in between 1 and10 positions, such as 1, 2, 3, 4, 5, 6, 7, 8, 9 or 10 positions of SEQID NO: 165. In one embodiment, the polypeptide preferably comprises orconsists of the amino acid sequence of SEQ ID NO: 165 or an allelicvariant thereof; comprises SEQ ID NO: 165 or an allelic variant thereofand a N-terminal and/or C-terminal His-tag and/or HQ-tag; or is afragment thereof having arabinofuranosidase activity and having at least90% of the length of SEQ ID NO: 165. In another embodiment, thepolypeptide comprises or consists of amino acids 1 to 361 of SEQ ID NO:165. In an embodiment, the polypeptide has been isolated.

In another embodiment, the composition comprises a GH62 polypeptidehaving arabinofuranosidase activity, wherein GH62 polypeptide havingarabinofuranosidase activity has a sequence identity to the maturepolypeptide of SEQ ID NO: 167 of at least 80%, e.g., at least 85%, atleast 86%, at least 87%, at least 88%, at least 89%, at least 90%, atleast 91%, at least 92%, at least 93%, at least 94%, at least 95%, atleast 96%, at least 97%, at least 98%, at least 99%, or 100%.

In one embodiment, the polypeptide comprises one or more amino acidsubstitutions, and/or one or more amino acid deletions, and/or one ormore amino acid insertions or any combination thereof in between 1 and10 positions, such as 1, 2, 3, 4, 5, 6, 7, 8, 9 or 10 positions of themature polypeptide of SEQ ID NO: 167. In one embodiment, the polypeptidepreferably comprises or consists of the amino acid sequence of SEQ IDNO: 167 or an allelic variant thereof; comprises the amino acid sequenceof SEQ ID NO: 167 and a N-terminal and/or C-terminal His-tag and/orHQ-tag; or is a fragment thereof having arabinofuranosidase activity andhaving at least 90% of the length of the mature polypeptide. In anotherembodiment, the polypeptide comprises or consists of the maturepolypeptide of SEQ ID NO: 167. In another embodiment, the polypeptidecomprises or consists of amino acids 1 to 373 of SEQ ID NO: 167. In anembodiment, the polypeptide has been isolated.

In an embodiment, the composition comprises a GH62 polypeptide havingarabinofuranosidase activity having a sequence identity to SEQ ID NO:168 of at least 80%. In an embodiment, the GH62 polypeptide has asequence identity to SEQ ID NO: 168 of at least 85%. In an embodiment,the GH62 polypeptide has a sequence identity to SEQ ID NO: 168 of atleast 86%. In an embodiment, the GH62 polypeptide has a sequenceidentity to SEQ ID NO: 168 of at least 87%. In an embodiment, the GH62polypeptide has a sequence identity to SEQ ID NO: 168 of at least 88%.In an embodiment, the GH62 polypeptide has a sequence identity to SEQ IDNO: 168 of at least 89%. In an embodiment, the GH62 polypeptide has asequence identity to SEQ ID NO: 168 of at least 90%. In an embodiment,the GH62 polypeptide has a sequence identity to SEQ ID NO: 168 of atleast 91%. In an embodiment, the GH62 polypeptide has a sequenceidentity to SEQ ID NO: 168 of at least 92%. In an embodiment, the GH62polypeptide has a sequence identity to SEQ ID NO: 168 of at least 93%.In an embodiment, the GH62 polypeptide has a sequence identity to SEQ IDNO: 168 of at least 94%. In an embodiment, the GH62 polypeptide has asequence identity to SEQ ID NO: 168 of at least 95%. In an embodiment,the GH62 polypeptide has a sequence identity to SEQ ID NO: 168 of atleast 96%. In an embodiment, the GH62 polypeptide has a sequenceidentity to SEQ ID NO: 168 of at least 97%. In an embodiment, the GH62polypeptide has a sequence identity to SEQ ID NO: 168 of at least 98%.In an embodiment, the GH62 polypeptide has a sequence identity to SEQ IDNO: 168 of at least 99%.

In one embodiment, the polypeptide comprises one or more amino acidsubstitutions, and/or one or more amino acid deletions, and/or one ormore amino acid insertions or any combination thereof in between 1 and10 positions, such as 1, 2, 3, 4, 5, 6, 7, 8, 9 or 10 positions of SEQID NO: 168. In one embodiment, the polypeptide preferably comprises orconsists of the amino acid sequence of SEQ ID NO: 168 or an allelicvariant thereof; comprises SEQ ID NO: 168 or an allelic variant thereofand a N-terminal and/or C-terminal His-tag and/or HQ-tag; or is afragment thereof having arabinofuranosidase activity and having at least90% of the length of SEQ ID NO: 168. In another embodiment, thepolypeptide comprises or consists of amino acids 1 to 373 of SEQ ID NO:168. In an embodiment, the polypeptide has been isolated.

In another embodiment, the composition comprises a GH62 polypeptidehaving arabinofuranosidase activity, wherein GH62 polypeptide havingarabinofuranosidase activity has a sequence identity to the maturepolypeptide of SEQ ID NO: 170 of at least 80%, e.g., at least 85%, atleast 86%, at least 87%, at least 88%, at least 89%, at least 90%, atleast 91%, at least 92%, at least 93%, at least 94%, at least 95%, atleast 96%, at least 97%, at least 98%, at least 99%, or 100%.

In one embodiment, the polypeptide comprises one or more amino acidsubstitutions, and/or one or more amino acid deletions, and/or one ormore amino acid insertions or any combination thereof in between 1 and10 positions, such as 1, 2, 3, 4, 5, 6, 7, 8, 9 or 10 positions of themature polypeptide of SEQ ID NO: 170. In one embodiment, the polypeptidepreferably comprises or consists of the amino acid sequence of SEQ IDNO: 170 or an allelic variant thereof; comprises the amino acid sequenceof SEQ ID NO: 170 and a N-terminal and/or C-terminal His-tag and/orHQ-tag; or is a fragment thereof having arabinofuranosidase activity andhaving at least 90% of the length of the mature polypeptide. In anotherembodiment, the polypeptide comprises or consists of the maturepolypeptide of SEQ ID NO: 170. In another embodiment, the polypeptidecomprises or consists of amino acids 1 to 302 of SEQ ID NO: 170. In anembodiment, the polypeptide has been isolated.

In an embodiment, the composition comprises a GH62 polypeptide havingarabinofuranosidase activity having a sequence identity to SEQ ID NO:171 of at least 80%. In an embodiment, the GH62 polypeptide has asequence identity to SEQ ID NO: 171 of at least 85%. In an embodiment,the GH62 polypeptide has a sequence identity to SEQ ID NO: 171 of atleast 86%. In an embodiment, the GH62 polypeptide has a sequenceidentity to SEQ ID NO: 171 of at least 87%. In an embodiment, the GH62polypeptide has a sequence identity to SEQ ID NO: 171 of at least 88%.In an embodiment, the GH62 polypeptide has a sequence identity to SEQ IDNO: 171 of at least 89%. In an embodiment, the GH62 polypeptide has asequence identity to SEQ ID NO: 171 of at least 90%. In an embodiment,the GH62 polypeptide has a sequence identity to SEQ ID NO: 171 of atleast 91%. In an embodiment, the GH62 polypeptide has a sequenceidentity to SEQ ID NO: 171 of at least 92%. In an embodiment, the GH62polypeptide has a sequence identity to SEQ ID NO: 171 of at least 93%.In an embodiment, the GH62 polypeptide has a sequence identity to SEQ IDNO: 171 of at least 94%. In an embodiment, the GH62 polypeptide has asequence identity to SEQ ID NO: 171 of at least 95%. In an embodiment,the GH62 polypeptide has a sequence identity to SEQ ID NO: 171 of atleast 96%. In an embodiment, the GH62 polypeptide has a sequenceidentity to SEQ ID NO: 171 of at least 97%. In an embodiment, the GH62polypeptide has a sequence identity to SEQ ID NO: 171 of at least 98%.In an embodiment, the GH62 polypeptide has a sequence identity to SEQ IDNO: 171 of at least 99%.

In one embodiment, the polypeptide comprises one or more amino acidsubstitutions, and/or one or more amino acid deletions, and/or one ormore amino acid insertions or any combination thereof in between 1 and10 positions, such as 1, 2, 3, 4, 5, 6, 7, 8, 9 or 10 positions of SEQID NO: 171. In one embodiment, the polypeptide preferably comprises orconsists of the amino acid sequence of SEQ ID NO: 171 or an allelicvariant thereof; comprises SEQ ID NO: 171 or an allelic variant thereofand a N-terminal and/or C-terminal His-tag and/or HQ-tag; or is afragment thereof having arabinofuranosidase activity and having at least90% of the length of SEQ ID NO: 171. In another embodiment, thepolypeptide comprises or consists of amino acids 1 to 302 of SEQ ID NO:171. In an embodiment, the polypeptide has been isolated.

In another embodiment, the composition comprises a GH62 polypeptidehaving arabinofuranosidase activity, wherein GH62 polypeptide havingarabinofuranosidase activity has a sequence identity to the maturepolypeptide of SEQ ID NO: 173 of at least 80%, e.g., at least 85%, atleast 86%, at least 87%, at least 88%, at least 89%, at least 90%, atleast 91%, at least 92%, at least 93%, at least 94%, at least 95%, atleast 96%, at least 97%, at least 98%, at least 99%, or 100%.

In one embodiment, the polypeptide comprises one or more amino acidsubstitutions, and/or one or more amino acid deletions, and/or one ormore amino acid insertions or any combination thereof in between 1 and10 positions, such as 1, 2, 3, 4, 5, 6, 7, 8, 9 or 10 positions of themature polypeptide of SEQ ID NO: 173. In one embodiment, the polypeptidepreferably comprises or consists of the amino acid sequence of SEQ IDNO: 173 or an allelic variant thereof; comprises the amino acid sequenceof SEQ ID NO: 173 and a N-terminal and/or C-terminal His-tag and/orHQ-tag; or is a fragment thereof having arabinofuranosidase activity andhaving at least 90% of the length of the mature polypeptide. In anotherembodiment, the polypeptide comprises or consists of the maturepolypeptide of SEQ ID NO: 173. In another embodiment, the polypeptidecomprises or consists of amino acids 1 to 364 of SEQ ID NO: 173. In anembodiment, the polypeptide has been isolated.

In an embodiment, the composition comprises a GH62 polypeptide havingarabinofuranosidase activity having a sequence identity to SEQ ID NO:174 of at least 80%. In an embodiment, the GH62 polypeptide has asequence identity to SEQ ID NO: 174 of at least 85%. In an embodiment,the GH62 polypeptide has a sequence identity to SEQ ID NO: 174 of atleast 86%. In an embodiment, the GH62 polypeptide has a sequenceidentity to SEQ ID NO: 174 of at least 87%. In an embodiment, the GH62polypeptide has a sequence identity to SEQ ID NO: 174 of at least 88%.In an embodiment, the GH62 polypeptide has a sequence identity to SEQ IDNO: 174 of at least 89%. In an embodiment, the GH62 polypeptide has asequence identity to SEQ ID NO: 174 of at least 90%. In an embodiment,the GH62 polypeptide has a sequence identity to SEQ ID NO: 174 of atleast 91%. In an embodiment, the GH62 polypeptide has a sequenceidentity to SEQ ID NO: 174 of at least 92%. In an embodiment, the GH62polypeptide has a sequence identity to SEQ ID NO: 174 of at least 93%.In an embodiment, the GH62 polypeptide has a sequence identity to SEQ IDNO: 174 of at least 94%. In an embodiment, the GH62 polypeptide has asequence identity to SEQ ID NO: 174 of at least 95%. In an embodiment,the GH62 polypeptide has a sequence identity to SEQ ID NO: 174 of atleast 96%. In an embodiment, the GH62 polypeptide has a sequenceidentity to SEQ ID NO: 174 of at least 97%. In an embodiment, the GH62polypeptide has a sequence identity to SEQ ID NO: 174 of at least 98%.In an embodiment, the GH62 polypeptide has a sequence identity to SEQ IDNO: 174 of at least 99%.

In one embodiment, the polypeptide comprises one or more amino acidsubstitutions, and/or one or more amino acid deletions, and/or one ormore amino acid insertions or any combination thereof in between 1 and10 positions, such as 1, 2, 3, 4, 5, 6, 7, 8, 9 or 10 positions of SEQID NO: 174. In one embodiment, the polypeptide preferably comprises orconsists of the amino acid sequence of SEQ ID NO: 174 or an allelicvariant thereof; comprises SEQ ID NO: 174 or an allelic variant thereofand a N-terminal and/or C-terminal His-tag and/or HQ-tag; or is afragment thereof having arabinofuranosidase activity and having at least90% of the length of SEQ ID NO: 174. In another embodiment, thepolypeptide comprises or consists of amino acids 1 to 364 of SEQ ID NO:174. In an embodiment, the polypeptide has been isolated.

GH10 and GH11 Polypeptides of the Composition

Preferred embodiments of the first aspect of the invention relating tothe GH10 or GH11 polypeptide having xylanase activity are disclosedherein below.

In an embodiment, the composition comprises a GH10 polypeptide havingxylanase activity such as the xylanase from Aspergillus aculeatus (XylII) as disclosed in WO 1994/021785 as SEQ ID NO: 5 and disclosed hereinas SEQ ID NO: 70.

In an embodiment, the composition comprises a GH10 polypeptide havingxylanase activity having a sequence identity to SEQ ID NO: 70 of atleast 80%. In an embodiment, the GH10 polypeptide has a sequenceidentity to SEQ ID NO: 70 of at least 85%. In an embodiment, the GH10polypeptide has a sequence identity to SEQ ID NO: 70 of at least 86%. Inan embodiment, the GH10 polypeptide has a sequence identity to SEQ IDNO: 70 of at least 87%. In an embodiment, the GH10 polypeptide has asequence identity to SEQ ID NO: 70 of at least 88%. In an embodiment,the GH10 polypeptide has a sequence identity to SEQ ID NO: 70 of atleast 89%. In an embodiment, the GH10 polypeptide has a sequenceidentity to SEQ ID NO: 70 of at least 90%. In an embodiment, the GH10polypeptide has a sequence identity to SEQ ID NO: 70 of at least 91%. Inan embodiment, the GH10 polypeptide has a sequence identity to SEQ IDNO: 70 of at least 92%. In an embodiment, the GH10 polypeptide has asequence identity to SEQ ID NO: 70 of at least 93%. In an embodiment,the GH10 polypeptide has a sequence identity to SEQ ID NO: 70 of atleast 94%. In an embodiment, the GH10 polypeptide has a sequenceidentity to SEQ ID NO: 70 of at least 95%. In an embodiment, the GH10polypeptide has a sequence identity to SEQ ID NO: 70 of at least 96%. Inan embodiment, the GH10 polypeptide has a sequence identity to SEQ IDNO: 70 of at least 97%. In an embodiment, the GH10 polypeptide has asequence identity to SEQ ID NO: 70 of at least 98%. In an embodiment,the GH10 polypeptide has a sequence identity to SEQ ID NO: 70 of atleast 99%.

In one embodiment, the polypeptide comprises one or more amino acidsubstitutions, and/or one or more amino acid deletions, and/or one ormore amino acid insertions or any combination thereof in between 1 and10 positions, such as 1, 2, 3, 4, 5, 6, 7, 8, 9 or 10 positions of SEQID NO: 70. In one embodiment, the polypeptide preferably comprises orconsists of the amino acid sequence of SEQ ID NO: 70 or an allelicvariant thereof; comprises SEQ ID NO: 70 or an allelic variant thereofand a N-terminal and/or C-terminal His-tag and/or HQ-tag; or is afragment thereof having xylanase activity and having at least 90% of thelength of SEQ ID NO: 70. In another embodiment, the polypeptidecomprises or consists of amino acids 1 to 384 of SEQ ID NO: 70. In anembodiment, the polypeptide has been isolated.

In an embodiment, the composition comprises a GH10 polypeptide havingxylanase activity such as the xylanase from Clostridium acetobutylicumas disclosed in J. Bacteriol. 2001, 183(16):4823 as Swissprot:Q97TP5 anddisclosed herein as SEQ ID NO: 71.

In an embodiment, the composition comprises a GH10 polypeptide havingxylanase activity having a sequence identity to SEQ ID NO: 71 of atleast 80%. In an embodiment, the GH10 polypeptide has a sequenceidentity to SEQ ID NO: 71 of at least 85%. In an embodiment, the GH10polypeptide has a sequence identity to SEQ ID NO: 71 of at least 86%. Inan embodiment, the GH10 polypeptide has a sequence identity to SEQ IDNO: 71 of at least 87%. In an embodiment, the GH10 polypeptide has asequence identity to SEQ ID NO: 71 of at least 88%. In an embodiment,the GH10 polypeptide has a sequence identity to SEQ ID NO: 71 of atleast 89%. In an embodiment, the GH10 polypeptide has a sequenceidentity to SEQ ID NO: 71 of at least 90%. In an embodiment, the GH10polypeptide has a sequence identity to SEQ ID NO: 71 of at least 91%. Inan embodiment, the GH10 polypeptide has a sequence identity to SEQ IDNO: 71 of at least 92%. In an embodiment, the GH10 polypeptide has asequence identity to SEQ ID NO: 71 of at least 93%. In an embodiment,the GH10 polypeptide has a sequence identity to SEQ ID NO: 71 of atleast 94%. In an embodiment, the GH10 polypeptide has a sequenceidentity to SEQ ID NO: 71 of at least 95%. In an embodiment, the GH10polypeptide has a sequence identity to SEQ ID NO: 71 of at least 96%. Inan embodiment, the GH10 polypeptide has a sequence identity to SEQ IDNO: 71 of at least 97%. In an embodiment, the GH10 polypeptide has asequence identity to SEQ ID NO: 71 of at least 98%. In an embodiment,the GH10 polypeptide has a sequence identity to SEQ ID NO: 71 of atleast 99%.

In one embodiment, the polypeptide comprises one or more amino acidsubstitutions, and/or one or more amino acid deletions, and/or one ormore amino acid insertions or any combination thereof in between 1 and10 positions, such as 1, 2, 3, 4, 5, 6, 7, 8, 9 or 10 positions of SEQID NO: 71. In one embodiment, the polypeptide preferably comprises orconsists of the amino acid sequence of SEQ ID NO: 71 or an allelicvariant thereof; comprises SEQ ID NO: 71 or an allelic variant thereofand a N-terminal and/or C-terminal His-tag and/or HQ-tag; or is afragment thereof having xylanase activity and having at least 90% of thelength of SEQ ID NO: 71. In another embodiment, the polypeptidecomprises or consists of amino acids 1 to 288 of SEQ ID NO: 71. In anembodiment, the polypeptide has been isolated.

In an embodiment, the composition comprises a GH10 polypeptide havingxylanase activity such as the xylanase from Aspergillus aculeatus asdisclosed as SEQ ID NO: 8 in WO 2005/059084 and disclosed herein as SEQID NO: 72.

In an embodiment, the composition comprises a GH10 polypeptide havingxylanase activity having a sequence identity to SEQ ID NO: 72 of atleast 80%. In an embodiment, the GH10 polypeptide has a sequenceidentity to SEQ ID NO: 72 of at least 85%. In an embodiment, the GH10polypeptide has a sequence identity to SEQ ID NO: 72 of at least 86%. Inan embodiment, the GH10 polypeptide has a sequence identity to SEQ IDNO: 72 of at least 87%. In an embodiment, the GH10 polypeptide has asequence identity to SEQ ID NO: 72 of at least 88%. In an embodiment,the GH10 polypeptide has a sequence identity to SEQ ID NO: 72 of atleast 89%. In an embodiment, the GH10 polypeptide has a sequenceidentity to SEQ ID NO: 72 of at least 90%. In an embodiment, the GH10polypeptide has a sequence identity to SEQ ID NO: 72 of at least 91%. Inan embodiment, the GH10 polypeptide has a sequence identity to SEQ IDNO: 72 of at least 92%. In an embodiment, the GH10 polypeptide has asequence identity to SEQ ID NO: 72 of at least 93%. In an embodiment,the GH10 polypeptide has a sequence identity to SEQ ID NO: 72 of atleast 94%. In an embodiment, the GH10 polypeptide has a sequenceidentity to SEQ ID NO: 72 of at least 95%. In an embodiment, the GH10polypeptide has a sequence identity to SEQ ID NO: 72 of at least 96%. Inan embodiment, the GH10 polypeptide has a sequence identity to SEQ IDNO: 72 of at least 97%. In an embodiment, the GH10 polypeptide has asequence identity to SEQ ID NO: 72 of at least 98%. In an embodiment,the GH10 polypeptide has a sequence identity to SEQ ID NO: 72 of atleast 99%.

In one embodiment, the polypeptide comprises one or more amino acidsubstitutions, and/or one or more amino acid deletions, and/or one ormore amino acid insertions or any combination thereof in between 1 and10 positions, such as 1, 2, 3, 4, 5, 6, 7, 8, 9 or 10 positions of SEQID NO: 72. In one embodiment, the polypeptide preferably comprises orconsists of the amino acid sequence of SEQ ID NO: 72 or an allelicvariant thereof; comprises SEQ ID NO: 72 or an allelic variant thereofand a N-terminal and/or C-terminal His-tag and/or HQ-tag; or is afragment thereof having xylanase activity and having at least 90% of thelength of SEQ ID NO: 72. In another embodiment, the polypeptidecomprises or consists of amino acids 1 to 308 of SEQ ID NO: 72. In anembodiment, the polypeptide has been isolated.

In an embodiment, the composition comprises a GH11 polypeptide havingxylanase activity such as the xylanase from Thermomyces lanuginosus asdisclosed as SEQ ID NO: 2 in WO1996/23062 and disclosed herein as SEQ IDNO: 73.

In an embodiment, the composition comprises a GH10 polypeptide havingxylanase activity having a sequence identity to SEQ ID NO: 73 of atleast 80%. In an embodiment, the GH10 polypeptide has a sequenceidentity to SEQ ID NO: 73 of at least 85%. In an embodiment, the GH10polypeptide has a sequence identity to SEQ ID NO: 73 of at least 86%. Inan embodiment, the GH10 polypeptide has a sequence identity to SEQ IDNO: 73 of at least 87%. In an embodiment, the GH10 polypeptide has asequence identity to SEQ ID NO: 73 of at least 88%. In an embodiment,the GH10 polypeptide has a sequence identity to SEQ ID NO: 73 of atleast 89%. In an embodiment, the GH10 polypeptide has a sequenceidentity to SEQ ID NO: 73 of at least 90%. In an embodiment, the GH10polypeptide has a sequence identity to SEQ ID NO: 73 of at least 91%. Inan embodiment, the GH10 polypeptide has a sequence identity to SEQ IDNO: 73 of at least 92%. In an embodiment, the GH10 polypeptide has asequence identity to SEQ ID NO: 73 of at least 93%. In an embodiment,the GH10 polypeptide has a sequence identity to SEQ ID NO: 73 of atleast 94%. In an embodiment, the GH10 polypeptide has a sequenceidentity to SEQ ID NO: 73 of at least 95%. In an embodiment, the GH10polypeptide has a sequence identity to SEQ ID NO: 73 of at least 96%. Inan embodiment, the GH10 polypeptide has a sequence identity to SEQ IDNO: 73 of at least 97%. In an embodiment, the GH10 polypeptide has asequence identity to SEQ ID NO: 73 of at least 98%. In an embodiment,the GH10 polypeptide has a sequence identity to SEQ ID NO: 73 of atleast 99%.

In one embodiment, the polypeptide comprises one or more amino acidsubstitutions, and/or one or more amino acid deletions, and/or one ormore amino acid insertions or any combination thereof in between 1 and10 positions, such as 1, 2, 3, 4, 5, 6, 7, 8, 9 or 10 positions of SEQID NO: 73. In one embodiment, the polypeptide preferably comprises orconsists of the amino acid sequence of SEQ ID NO: 73 or an allelicvariant thereof; comprises SEQ ID NO: 73 or an allelic variant thereofand a N-terminal and/or C-terminal His-tag and/or HQ-tag; or is afragment thereof having xylanase activity and having at least 90% of thelength of SEQ ID NO: 73. In another embodiment, the polypeptidecomprises or consists of amino acids 1 to 195 of SEQ ID NO: 73. In anembodiment, the polypeptide has been isolated.

In an embodiment, the composition comprises a GH11 polypeptide havingxylanase activity such as the xylanase from Dictyoglomus thermophilum asdisclosed as SEQ ID NO: 305 in WO2011/057140 and disclosed herein as SEQID NO: 74.

In an embodiment, the composition comprises a GH10 polypeptide havingxylanase activity having a sequence identity to SEQ ID NO: 74 of atleast 80%. In an embodiment, the GH10 polypeptide has a sequenceidentity to SEQ ID NO: 74 of at least 85%. In an embodiment, the GH10polypeptide has a sequence identity to SEQ ID NO: 74 of at least 86%. Inan embodiment, the GH10 polypeptide has a sequence identity to SEQ IDNO: 74 of at least 87%. In an embodiment, the GH10 polypeptide has asequence identity to SEQ ID NO: 74 of at least 88%. In an embodiment,the GH10 polypeptide has a sequence identity to SEQ ID NO: 74 of atleast 89%. In an embodiment, the GH10 polypeptide has a sequenceidentity to SEQ ID NO: 74 of at least 90%. In an embodiment, the GH10polypeptide has a sequence identity to SEQ ID NO: 74 of at least 91%. Inan embodiment, the GH10 polypeptide has a sequence identity to SEQ IDNO: 74 of at least 92%. In an embodiment, the GH10 polypeptide has asequence identity to SEQ ID NO: 74 of at least 93%. In an embodiment,the GH10 polypeptide has a sequence identity to SEQ ID NO: 74 of atleast 94%. In an embodiment, the GH10 polypeptide has a sequenceidentity to SEQ ID NO: 74 of at least 95%. In an embodiment, the GH10polypeptide has a sequence identity to SEQ ID NO: 74 of at least 96%. Inan embodiment, the GH10 polypeptide has a sequence identity to SEQ IDNO: 74 of at least 97%. In an embodiment, the GH10 polypeptide has asequence identity to SEQ ID NO: 74 of at least 98%. In an embodiment,the GH10 polypeptide has a sequence identity to SEQ ID NO: 74 of atleast 99%.

In one embodiment, the polypeptide comprises one or more amino acidsubstitutions, and/or one or more amino acid deletions, and/or one ormore amino acid insertions or any combination thereof in between 1 and10 positions, such as 1, 2, 3, 4, 5, 6, 7, 8, 9 or 10 positions of SEQID NO: 74. In one embodiment, the polypeptide preferably comprises orconsists of the amino acid sequence of SEQ ID NO: 74 or an allelicvariant thereof; comprises SEQ ID NO: 74 or an allelic variant thereofand a N-terminal and/or C-terminal His-tag and/or HQ-tag; or is afragment thereof having xylanase activity and having at least 90% of thelength of SEQ ID NO: 74. In another embodiment, the polypeptidecomprises or consists of amino acids 1 to 203 of SEQ ID NO: 74. In anembodiment, the polypeptide has been isolated.

In an embodiment, the composition comprises a GH11 polypeptide havingxylanase activity such as the xylanase from Paenibacillus Pabuli asdisclosed as SEQ ID NO: 2 in WO2005/079585 and disclosed herein as SEQID NO: 75.

In an embodiment, the composition comprises a GH10 polypeptide havingxylanase activity having a sequence identity to SEQ ID NO: 75 of atleast 80%. In an embodiment, the GH10 polypeptide has a sequenceidentity to SEQ ID NO: 75 of at least 85%. In an embodiment, the GH10polypeptide has a sequence identity to SEQ ID NO: 75 of at least 86%. Inan embodiment, the GH10 polypeptide has a sequence identity to SEQ IDNO: 75 of at least 87%. In an embodiment, the GH10 polypeptide has asequence identity to SEQ ID NO: 75 of at least 88%. In an embodiment,the GH10 polypeptide has a sequence identity to SEQ ID NO: 75 of atleast 89%. In an embodiment, the GH10 polypeptide has a sequenceidentity to SEQ ID NO: 75 of at least 90%. In an embodiment, the GH10polypeptide has a sequence identity to SEQ ID NO: 75 of at least 91%. Inan embodiment, the GH10 polypeptide has a sequence identity to SEQ IDNO: 75 of at least 92%. In an embodiment, the GH10 polypeptide has asequence identity to SEQ ID NO: 75 of at least 93%. In an embodiment,the GH10 polypeptide has a sequence identity to SEQ ID NO: 75 of atleast 94%. In an embodiment, the GH10 polypeptide has a sequenceidentity to SEQ ID NO: 75 of at least 95%. In an embodiment, the GH10polypeptide has a sequence identity to SEQ ID NO: 75 of at least 96%. Inan embodiment, the GH10 polypeptide has a sequence identity to SEQ IDNO: 75 of at least 97%. In an embodiment, the GH10 polypeptide has asequence identity to SEQ ID NO: 75 of at least 98%. In an embodiment,the GH10 polypeptide has a sequence identity to SEQ ID NO: 75 of atleast 99%.

In one embodiment, the polypeptide comprises one or more amino acidsubstitutions, and/or one or more amino acid deletions, and/or one ormore amino acid insertions or any combination thereof in between 1 and10 positions, such as 1, 2, 3, 4, 5, 6, 7, 8, 9 or 10 positions of SEQID NO: 75. In one embodiment, the polypeptide preferably comprises orconsists of the amino acid sequence of SEQ ID NO: 75 or an allelicvariant thereof; comprises SEQ ID NO: 75 or an allelic variant thereofand a N-terminal and/or C-terminal His-tag and/or HQ-tag; or is afragment thereof having xylanase activity and having at least 90% of thelength of SEQ ID NO: 75. In another embodiment, the polypeptidecomprises or consists of amino acids 1 to 182 of SEQ ID NO: 75. In anembodiment, the polypeptide has been isolated.

In an embodiment, the composition comprises a GH11 polypeptide havingxylanase activity such as the xylanase from Geobacillusstearothermophilus as disclosed herein as SEQ ID NO: 78. In anembodiment, the composition comprises a GH10 polypeptide having xylanaseactivity having a sequence identity to the mature polypeptide of SEQ IDNO: 77 of at least 80%, e.g., at least 85%, at least 86%, at least 87%,at least 88%, at least 89%, at least 90%, at least 91%, at least 92%, atleast 93%, at least 94%, at least 95%, at least 96%, at least 97%, atleast 98%, at least 99%, or 100%.

In one embodiment, the polypeptide comprises one or more amino acidsubstitutions, and/or one or more amino acid deletions, and/or one ormore amino acid insertions or any combination thereof in between 1 and10 positions, such as 1, 2, 3, 4, 5, 6, 7, 8, 9 or 10 positions of themature polypeptide of SEQ ID NO: 77. In one embodiment, the polypeptidepreferably comprises or consists of the amino acid sequence of SEQ IDNO: 77 or an allelic variant thereof; comprises the amino acid sequenceof SEQ ID NO: 77 and a N-terminal and/or C-terminal His-tag and/orHQ-tag such as the mature polypeptide of SEQ ID NO: 80 or SEQ ID NO: 81;or is a fragment thereof having xylanase activity and having at least90% of the length of the mature polypeptide. In another embodiment, thepolypeptide comprises or consists of the mature polypeptide of SEQ IDNO: 77. In another embodiment, the polypeptide comprises or consists ofamino acids 1 to 183 of SEQ ID NO: 77. In another embodiment, thepolypeptide comprises or consists of the mature polypeptide of SEQ IDNO: 80. In another embodiment, the polypeptide comprises or consists ofamino acids 1 to 181 of SEQ ID NO: 80. In an embodiment, the polypeptidehas been isolated.

In an embodiment, the composition comprises a GH10 polypeptide havingxylanase activity having a sequence identity to SEQ ID NO: 78 of atleast 80%. In an embodiment, the GH10 polypeptide has a sequenceidentity to SEQ ID NO: 78 of at least 85%. In an embodiment, the GH10polypeptide has a sequence identity to SEQ ID NO: 78 of at least 86%. Inan embodiment, the GH10 polypeptide has a sequence identity to SEQ IDNO: 78 of at least 87%. In an embodiment, the GH10 polypeptide has asequence identity to SEQ ID NO: 78 of at least 88%. In an embodiment,the GH10 polypeptide has a sequence identity to SEQ ID NO: 78 of atleast 89%. In an embodiment, the GH10 polypeptide has a sequenceidentity to SEQ ID NO: 78 of at least 90%. In an embodiment, the GH10polypeptide has a sequence identity to SEQ ID NO: 78 of at least 91%. Inan embodiment, the GH10 polypeptide has a sequence identity to SEQ IDNO: 78 of at least 92%. In an embodiment, the GH10 polypeptide has asequence identity to SEQ ID NO: 78 of at least 93%. In an embodiment,the GH10 polypeptide has a sequence identity to SEQ ID NO: 78 of atleast 94%. In an embodiment, the GH10 polypeptide has a sequenceidentity to SEQ ID NO: 78 of at least 95%. In an embodiment, the GH10polypeptide has a sequence identity to SEQ ID NO: 78 of at least 96%. Inan embodiment, the GH10 polypeptide has a sequence identity to SEQ IDNO: 78 of at least 97%. In an embodiment, the GH10 polypeptide has asequence identity to SEQ ID NO: 78 of at least 98%. In an embodiment,the GH10 polypeptide has a sequence identity to SEQ ID NO: 78 of atleast 99%.

In one embodiment, the polypeptide comprises one or more amino acidsubstitutions, and/or one or more amino acid deletions, and/or one ormore amino acid insertions or any combination thereof in between 1 and10 positions, such as 1, 2, 3, 4, 5, 6, 7, 8, 9 or 10 positions of SEQID NO: 78. In one embodiment, the polypeptide comprises one or moreamino acid substitutions, and/or one or more amino acid deletions,and/or one or more amino acid insertions or any combination thereof inbetween 1 and 10 positions, such as 1, 2, 3, 4, 5, 6, 7, 8, 9 or 10positions of SEQ ID NO: 81. In one embodiment, the polypeptidepreferably comprises or consists of the amino acid sequence of SEQ IDNO: 78 or an allelic variant thereof; comprises SEQ ID NO: 78 or anallelic variant thereof and a N-terminal and/or C-terminal His-tagand/or HQ-tag such as SEQ ID NO: 81; or is a fragment thereof havingxylanase activity and having at least 90% of the length of SEQ ID NO:78. In another embodiment, the polypeptide comprises or consists ofamino acids 1 to 183 of SEQ ID NO: 78. In another embodiment, thepolypeptide comprises or consists of amino acids 1 to 181 of SEQ ID NO:81. In an embodiment, the polypeptide has been isolated.

In an embodiment, the composition comprises a GH11 polypeptide havingxylanase activity such as the xylanase from Streptomyces beijiangensisas disclosed herein as SEQ ID NO: 84. In an embodiment, the compositioncomprises a GH10 polypeptide having xylanase activity having a sequenceidentity to the mature polypeptide of SEQ ID NO: 83 of at least 80%,e.g., at least 85%, at least 86%, at least 87%, at least 88%, at least89%, at least 90%, at least 91%, at least 92%, at least 93%, at least94%, at least 95%, at least 96%, at least 97%, at least 98%, at least99%, or 100%.

In one embodiment, the polypeptide comprises one or more amino acidsubstitutions, and/or one or more amino acid deletions, and/or one ormore amino acid insertions or any combination thereof in between 1 and10 positions, such as 1, 2, 3, 4, 5, 6, 7, 8, 9 or 10 positions of themature polypeptide of SEQ ID NO: 83. In one embodiment, the polypeptidepreferably comprises or consists of the amino acid sequence of SEQ IDNO: 83 or an allelic variant thereof; comprises the amino acid sequenceof SEQ ID NO: 83 and a N-terminal and/or C-terminal His-tag and/orHQ-tag such as the mature polypeptide of SEQ ID NO: 86 or SEQ ID NO: 87;or is a fragment thereof having xylanase activity and having at least90% of the length of the mature polypeptide. In another embodiment, thepolypeptide comprises or consists of the mature polypeptide of SEQ IDNO: 83. In another embodiment, the polypeptide comprises or consists ofamino acids 1 to 299 of SEQ ID NO: 83. In another embodiment, thepolypeptide comprises or consists of the mature polypeptide of SEQ IDNO: 86. In another embodiment, the polypeptide comprises or consists ofamino acids 1 to 307 of SEQ ID NO: 86. In an embodiment, the polypeptidehas been isolated.

In an embodiment, the composition comprises a GH10 polypeptide havingxylanase activity having a sequence identity to SEQ ID NO: 84 of atleast 80%. In an embodiment, the GH10 polypeptide has a sequenceidentity to SEQ ID NO: 84 of at least 85%. In an embodiment, the GH10polypeptide has a sequence identity to SEQ ID NO: 84 of at least 86%. Inan embodiment, the GH10 polypeptide has a sequence identity to SEQ IDNO: 84 of at least 87%. In an embodiment, the GH10 polypeptide has asequence identity to SEQ ID NO: 84 of at least 88%. In an embodiment,the GH10 polypeptide has a sequence identity to SEQ ID NO: 84 of atleast 89%. In an embodiment, the GH10 polypeptide has a sequenceidentity to SEQ ID NO: 84 of at least 90%. In an embodiment, the GH10polypeptide has a sequence identity to SEQ ID NO: 84 of at least 91%. Inan embodiment, the GH10 polypeptide has a sequence identity to SEQ IDNO: 84 of at least 92%. In an embodiment, the GH10 polypeptide has asequence identity to SEQ ID NO: 84 of at least 93%. In an embodiment,the GH10 polypeptide has a sequence identity to SEQ ID NO: 84 of atleast 94%. In an embodiment, the GH10 polypeptide has a sequenceidentity to SEQ ID NO: 84 of at least 95%. In an embodiment, the GH10polypeptide has a sequence identity to SEQ ID NO: 84 of at least 96%. Inan embodiment, the GH10 polypeptide has a sequence identity to SEQ IDNO: 84 of at least 97%. In an embodiment, the GH10 polypeptide has asequence identity to SEQ ID NO: 84 of at least 98%. In an embodiment,the GH10 polypeptide has a sequence identity to SEQ ID NO: 84 of atleast 99%.

In one embodiment, the polypeptide comprises one or more amino acidsubstitutions, and/or one or more amino acid deletions, and/or one ormore amino acid insertions or any combination thereof in between 1 and10 positions, such as 1, 2, 3, 4, 5, 6, 7, 8, 9 or 10 positions of SEQID NO: 84. In one embodiment, the polypeptide comprises one or moreamino acid substitutions, and/or one or more amino acid deletions,and/or one or more amino acid insertions or any combination thereof inbetween 1 and 10 positions, such as 1, 2, 3, 4, 5, 6, 7, 8, 9 or 10positions of SEQ ID NO: 87. In one embodiment, the polypeptidepreferably comprises or consists of the amino acid sequence of SEQ IDNO: 84 or an allelic variant thereof; comprises SEQ ID NO: 84 or anallelic variant thereof and a N-terminal and/or C-terminal His-tagand/or HQ-tag such as SEQ ID NO: 87; or is a fragment thereof havingxylanase activity and having at least 90% of the length of SEQ ID NO:84. In another embodiment, the polypeptide comprises or consists ofamino acids 1 to 299 of SEQ ID NO: 84. In another embodiment, thepolypeptide comprises or consists of amino acids 1 to 307 of SEQ ID NO:87. In an embodiment, the polypeptide has been isolated.

In an embodiment, the composition comprises a GH11 polypeptide havingxylanase activity such as the xylanase from Fusarium oxysporum calledFoxXyn6 as disclosed as SEQ ID NO: 2 in WO2014/019220 and as disclosedherein as SEQ ID NO: 88.

In an embodiment, the composition comprises a GH10 polypeptide havingxylanase activity having a sequence identity to SEQ ID NO: 88 of atleast 80%. In an embodiment, the GH10 polypeptide has a sequenceidentity to SEQ ID NO: 88 of at least 85%. In an embodiment, the GH10polypeptide has a sequence identity to SEQ ID NO: 88 of at least 86%. Inan embodiment, the GH10 polypeptide has a sequence identity to SEQ IDNO: 88 of at least 87%. In an embodiment, the GH10 polypeptide has asequence identity to SEQ ID NO: 88 of at least 88%. In an embodiment,the GH10 polypeptide has a sequence identity to SEQ ID NO: 88 of atleast 89%. In an embodiment, the GH10 polypeptide has a sequenceidentity to SEQ ID NO: 88 of at least 90%. In an embodiment, the GH10polypeptide has a sequence identity to SEQ ID NO: 88 of at least 91%. Inan embodiment, the GH10 polypeptide has a sequence identity to SEQ IDNO: 88 of at least 92%. In an embodiment, the GH10 polypeptide has asequence identity to SEQ ID NO: 88 of at least 93%. In an embodiment,the GH10 polypeptide has a sequence identity to SEQ ID NO: 88 of atleast 94%. In an embodiment, the GH10 polypeptide has a sequenceidentity to SEQ ID NO: 88 of at least 95%. In an embodiment, the GH10polypeptide has a sequence identity to SEQ ID NO: 88 of at least 96%. Inan embodiment, the GH10 polypeptide has a sequence identity to SEQ IDNO: 88 of at least 97%. In an embodiment, the GH10 polypeptide has asequence identity to SEQ ID NO: 88 of at least 98%. In an embodiment,the GH10 polypeptide has a sequence identity to SEQ ID NO: 88 of atleast 99%.

In one embodiment, the polypeptide comprises one or more amino acidsubstitutions, and/or one or more amino acid deletions, and/or one ormore amino acid insertions or any combination thereof in between 1 and10 positions, such as 1, 2, 3, 4, 5, 6, 7, 8, 9 or 10 positions of SEQID NO: 88. In one embodiment, the polypeptide preferably comprises orconsists of the amino acid sequence of SEQ ID NO: 88 or an allelicvariant thereof; comprises SEQ ID NO: 88 or an allelic variant thereofand a N-terminal and/or C-terminal His-tag and/or HQ-tag; or is afragment thereof having xylanase activity and having at least 90% of thelength of SEQ ID NO: 88. In another embodiment, the polypeptidecomprises or consists of amino acids 1 to 188 of SEQ ID NO: 88. In anembodiment, the polypeptide has been isolated.

In an embodiment, the composition comprises a GH11 polypeptide havingxylanase activity such as the xylanase from Fusarium oxysporum calledAcIXyn5 as disclosed as SEQ ID NO: 7 in WO2014/020143 and as disclosedherein as SEQ ID NO: 89.

In an embodiment, the composition comprises a GH10 polypeptide havingxylanase activity having a sequence identity to SEQ ID NO: 89 of atleast 80%. In an embodiment, the GH10 polypeptide has a sequenceidentity to SEQ ID NO: 89 of at least 85%. In an embodiment, the GH10polypeptide has a sequence identity to SEQ ID NO: 89 of at least 86%. Inan embodiment, the GH10 polypeptide has a sequence identity to SEQ IDNO: 89 of at least 87%. In an embodiment, the GH10 polypeptide has asequence identity to SEQ ID NO: 89 of at least 88%. In an embodiment,the GH10 polypeptide has a sequence identity to SEQ ID NO: 89 of atleast 89%. In an embodiment, the GH10 polypeptide has a sequenceidentity to SEQ ID NO: 89 of at least 90%. In an embodiment, the GH10polypeptide has a sequence identity to SEQ ID NO: 89 of at least 91%. Inan embodiment, the GH10 polypeptide has a sequence identity to SEQ IDNO: 89 of at least 92%. In an embodiment, the GH10 polypeptide has asequence identity to SEQ ID NO: 89 of at least 93%. In an embodiment,the GH10 polypeptide has a sequence identity to SEQ ID NO: 89 of atleast 94%. In an embodiment, the GH10 polypeptide has a sequenceidentity to SEQ ID NO: 89 of at least 95%. In an embodiment, the GH10polypeptide has a sequence identity to SEQ ID NO: 89 of at least 96%. Inan embodiment, the GH10 polypeptide has a sequence identity to SEQ IDNO: 89 of at least 97%. In an embodiment, the GH10 polypeptide has asequence identity to SEQ ID NO: 89 of at least 98%. In an embodiment,the GH10 polypeptide has a sequence identity to SEQ ID NO: 89 of atleast 99%.

In one embodiment, the polypeptide comprises one or more amino acidsubstitutions, and/or one or more amino acid deletions, and/or one ormore amino acid insertions or any combination thereof in between 1 and10 positions, such as 1, 2, 3, 4, 5, 6, 7, 8, 9 or 10 positions of SEQID NO: 89. In one embodiment, the polypeptide preferably comprises orconsists of the amino acid sequence of SEQ ID NO: 89 or an allelicvariant thereof; comprises SEQ ID NO: 89 or an allelic variant thereofand a N-terminal and/or C-terminal His-tag and/or HQ-tag; or is afragment thereof having xylanase activity and having at least 90% of thelength of SEQ ID NO: 89. In another embodiment, the polypeptidecomprises or consists of amino acids 1 to 189 of SEQ ID NO: 89. In anembodiment, the polypeptide has been isolated.

In an embodiment, the composition comprises a GH10 polypeptide havingxylanase activity such as the xylanase from Thermotoga maritima MSB8called XynB as disclosed as SEQ ID NO: 1 in WO2013/068550 and asdisclosed herein as SEQ ID NO: 95.

In an embodiment, the composition comprises a GH10 polypeptide havingxylanase activity having a sequence identity to SEQ ID NO: 95 of atleast 80%. In an embodiment, the GH10 polypeptide has a sequenceidentity to SEQ ID NO: 95 of at least 85%. In an embodiment, the GH10polypeptide has a sequence identity to SEQ ID NO: 95 of at least 86%. Inan embodiment, the GH10 polypeptide has a sequence identity to SEQ IDNO: 95 of at least 87%. In an embodiment, the GH10 polypeptide has asequence identity to SEQ ID NO: 95 of at least 88%. In an embodiment,the GH10 polypeptide has a sequence identity to SEQ ID NO: 95 of atleast 89%. In an embodiment, the GH10 polypeptide has a sequenceidentity to SEQ ID NO: 95 of at least 90%. In an embodiment, the GH10polypeptide has a sequence identity to SEQ ID NO: 95 of at least 91%. Inan embodiment, the GH10 polypeptide has a sequence identity to SEQ IDNO: 95 of at least 92%. In an embodiment, the GH10 polypeptide has asequence identity to SEQ ID NO: 95 of at least 93%. In an embodiment,the GH10 polypeptide has a sequence identity to SEQ ID NO: 95 of atleast 94%. In an embodiment, the GH10 polypeptide has a sequenceidentity to SEQ ID NO: 95 of at least 95%. In an embodiment, the GH10polypeptide has a sequence identity to SEQ ID NO: 95 of at least 96%. Inan embodiment, the GH10 polypeptide has a sequence identity to SEQ IDNO: 95 of at least 97%. In an embodiment, the GH10 polypeptide has asequence identity to SEQ ID NO: 95 of at least 98%. In an embodiment,the GH10 polypeptide has a sequence identity to SEQ ID NO: 95 of atleast 99%.

In one embodiment, the polypeptide comprises one or more amino acidsubstitutions, and/or one or more amino acid deletions, and/or one ormore amino acid insertions or any combination thereof in between 1 and10 positions, such as 1, 2, 3, 4, 5, 6, 7, 8, 9 or 10 positions of SEQID NO: 95. In one embodiment, the polypeptide preferably comprises orconsists of the amino acid sequence of SEQ ID NO: 95 or an allelicvariant thereof; comprises SEQ ID NO: 95 or an allelic variant thereofand a N-terminal and/or C-terminal His-tag and/or HQ-tag; or is afragment thereof having xylanase activity and having at least 90% of thelength of SEQ ID NO: 95. In another embodiment, the polypeptidecomprises or consists of amino acids 1 to 328 of SEQ ID NO: 95. In anembodiment, the polypeptide has been isolated.

In an embodiment, the composition comprises a GH11 polypeptide havingxylanase activity such as the xylanase from Myceliophthora thermophilacalled Xyl6 as disclosed as SEQ ID NO: 41 in WO2009/018537 and asdisclosed herein as SEQ ID NO: 96.

In an embodiment, the composition comprises a GH11 polypeptide havingxylanase activity having a sequence identity to SEQ ID NO: 96 of atleast 80%. In an embodiment, the GH11 polypeptide has a sequenceidentity to SEQ ID NO: 96 of at least 85%. In an embodiment, the GH11polypeptide has a sequence identity to SEQ ID NO: 96 of at least 86%. Inan embodiment, the GH11 polypeptide has a sequence identity to SEQ IDNO: 96 of at least 87%. In an embodiment, the GH11 polypeptide has asequence identity to SEQ ID NO: 96 of at least 88%. In an embodiment,the GH11 polypeptide has a sequence identity to SEQ ID NO: 96 of atleast 89%. In an embodiment, the GH11 polypeptide has a sequenceidentity to SEQ ID NO: 96 of at least 90%. In an embodiment, the GH11polypeptide has a sequence identity to SEQ ID NO: 96 of at least 91%. Inan embodiment, the GH11 polypeptide has a sequence identity to SEQ IDNO: 96 of at least 92%. In an embodiment, the GH11 polypeptide has asequence identity to SEQ ID NO: 96 of at least 93%. In an embodiment,the GH11 polypeptide has a sequence identity to SEQ ID NO: 96 of atleast 94%. In an embodiment, the GH11 polypeptide has a sequenceidentity to SEQ ID NO: 96 of at least 95%. In an embodiment, the GH11polypeptide has a sequence identity to SEQ ID NO: 96 of at least 96%. Inan embodiment, the GH11 polypeptide has a sequence identity to SEQ IDNO: 96 of at least 97%. In an embodiment, the GH11 polypeptide has asequence identity to SEQ ID NO: 96 of at least 98%. In an embodiment,the GH11 polypeptide has a sequence identity to SEQ ID NO: 96 of atleast 99%.

In one embodiment, the polypeptide comprises one or more amino acidsubstitutions, and/or one or more amino acid deletions, and/or one ormore amino acid insertions or any combination thereof in between 1 and10 positions, such as 1, 2, 3, 4, 5, 6, 7, 8, 9 or 10 positions of SEQID NO: 96. In one embodiment, the polypeptide preferably comprises orconsists of the amino acid sequence of SEQ ID NO: 96 or an allelicvariant thereof; comprises SEQ ID NO: 96 or an allelic variant thereofand a N-terminal and/or C-terminal His-tag and/or HQ-tag; or is afragment thereof having xylanase activity and having at least 90% of thelength of SEQ ID NO: 96. In another embodiment, the polypeptidecomprises or consists of amino acids 1 to 208 of SEQ ID NO: 96. In anembodiment, the polypeptide has been isolated.

In an embodiment, the composition comprises a GH11 polypeptide havingxylanase activity, wherein GH11 polypeptide having xylanase activity hasa sequence identity to the mature polypeptide of SEQ ID NO: 98 of atleast 80%, e.g., at least 85%, at least 86%, at least 87%, at least 88%,at least 89%, at least 90%, at least 91%, at least 92%, at least 93%, atleast 94%, at least 95%, at least 96%, at least 97%, at least 98%, atleast 99%, or 100%.

In one embodiment, the polypeptide comprises one or more amino acidsubstitutions, and/or one or more amino acid deletions, and/or one ormore amino acid insertions or any combination thereof in between 1 and10 positions, such as 1, 2, 3, 4, 5, 6, 7, 8, 9 or 10 positions of themature polypeptide of SEQ ID NO: 98. In one embodiment, the polypeptidepreferably comprises or consists of the amino acid sequence of SEQ IDNO: 98 or an allelic variant thereof; comprises the amino acid sequenceof SEQ ID NO: 98 and a N-terminal and/or C-terminal His-tag and/orHQ-tag; or is a fragment thereof having xylanase activity and having atleast 90% of the length of the mature polypeptide. In anotherembodiment, the polypeptide comprises or consists of the maturepolypeptide of SEQ ID NO: 98. In another embodiment, the polypeptidecomprises or consists of amino acids 1 to 203 of SEQ ID NO: 98. In anembodiment, the polypeptide has been isolated.

In an embodiment, the composition comprises a GH11 polypeptide havingxylanase activity having a sequence identity to SEQ ID NO: 99 of atleast 80%. In an embodiment, the GH11 polypeptide has a sequenceidentity to SEQ ID NO: 99 of at least 85%. In an embodiment, the GH11polypeptide has a sequence identity to SEQ ID NO: 99 of at least 86%. Inan embodiment, the GH11 polypeptide has a sequence identity to SEQ IDNO: 99 of at least 87%. In an embodiment, the GH11 polypeptide has asequence identity to SEQ ID NO: 99 of at least 88%. In an embodiment,the GH11 polypeptide has a sequence identity to SEQ ID NO: 99 of atleast 89%. In an embodiment, the GH11 polypeptide has a sequenceidentity to SEQ ID NO: 99 of at least 90%. In an embodiment, the GH11polypeptide has a sequence identity to SEQ ID NO: 99 of at least 91%. Inan embodiment, the GH11 polypeptide has a sequence identity to SEQ IDNO: 99 of at least 92%. In an embodiment, the GH11 polypeptide has asequence identity to SEQ ID NO: 99 of at least 93%. In an embodiment,the GH11 polypeptide has a sequence identity to SEQ ID NO: 99 of atleast 94%. In an embodiment, the GH11 polypeptide has a sequenceidentity to SEQ ID NO: 99 of at least 95%. In an embodiment, the GH11polypeptide has a sequence identity to SEQ ID NO: 99 of at least 96%. Inan embodiment, the GH11 polypeptide has a sequence identity to SEQ IDNO: 99 of at least 97%. In an embodiment, the GH11 polypeptide has asequence identity to SEQ ID NO: 99 of at least 98%. In an embodiment,the GH11 polypeptide has a sequence identity to SEQ ID NO: 99 of atleast 99%.

In one embodiment, the polypeptide comprises one or more amino acidsubstitutions, and/or one or more amino acid deletions, and/or one ormore amino acid insertions or any combination thereof in between 1 and10 positions, such as 1, 2, 3, 4, 5, 6, 7, 8, 9 or 10 positions of SEQID NO: 99. In one embodiment, the polypeptide preferably comprises orconsists of the amino acid sequence of SEQ ID NO: 99 or an allelicvariant thereof; comprises SEQ ID NO: 99 or an allelic variant thereofand a N-terminal and/or C-terminal His-tag and/or HQ-tag; or is afragment thereof having xylanase activity and having at least 90% of thelength of SEQ ID NO: 99. In another embodiment, the polypeptidecomprises or consists of amino acids 1 to 203 of SEQ ID NO: 99. In anembodiment, the polypeptide has been isolated.

In an embodiment, the composition comprises a GH10 polypeptide havingxylanase activity, wherein GH10 polypeptide having xylanase activity hasa sequence identity to the mature polypeptide of SEQ ID NO: 101 of atleast 80%, e.g., at least 85%, at least 86%, at least 87%, at least 88%,at least 89%, at least 90%, at least 91%, at least 92%, at least 93%, atleast 94%, at least 95%, at least 96%, at least 97%, at least 98%, atleast 99%, or 100%.

In one embodiment, the polypeptide comprises one or more amino acidsubstitutions, and/or one or more amino acid deletions, and/or one ormore amino acid insertions or any combination thereof in between 1 and10 positions, such as 1, 2, 3, 4, 5, 6, 7, 8, 9 or 10 positions of themature polypeptide of SEQ ID NO: 101. In one embodiment, the polypeptidepreferably comprises or consists of the amino acid sequence of SEQ IDNO: 101 or an allelic variant thereof; comprises the amino acid sequenceof SEQ ID NO: 101 and a N-terminal and/or C-terminal His-tag and/orHQ-tag; or is a fragment thereof having xylanase activity and having atleast 90% of the length of the mature polypeptide. In anotherembodiment, the polypeptide comprises or consists of the maturepolypeptide of SEQ ID NO: 101. In another embodiment, the polypeptidecomprises or consists of amino acids 1 to 337 of SEQ ID NO: 101. In anembodiment, the polypeptide has been isolated.

In an embodiment, the composition comprises a GH10 polypeptide havingxylanase activity having a sequence identity to SEQ ID NO: 102 of atleast 80%. In an embodiment, the GH10 polypeptide has a sequenceidentity to SEQ ID NO: 102 of at least 85%. In an embodiment, the GH10polypeptide has a sequence identity to SEQ ID NO: 102 of at least 86%.In an embodiment, the GH10 polypeptide has a sequence identity to SEQ IDNO: 102 of at least 87%. In an embodiment, the GH10 polypeptide has asequence identity to SEQ ID NO: 102 of at least 88%. In an embodiment,the GH10 polypeptide has a sequence identity to SEQ ID NO: 102 of atleast 89%. In an embodiment, the GH10 polypeptide has a sequenceidentity to SEQ ID NO: 102 of at least 90%. In an embodiment, the GH10polypeptide has a sequence identity to SEQ ID NO: 102 of at least 91%.In an embodiment, the GH10 polypeptide has a sequence identity to SEQ IDNO: 102 of at least 92%. In an embodiment, the GH10 polypeptide has asequence identity to SEQ ID NO: 102 of at least 93%. In an embodiment,the GH10 polypeptide has a sequence identity to SEQ ID NO: 102 of atleast 94%. In an embodiment, the GH10 polypeptide has a sequenceidentity to SEQ ID NO: 102 of at least 95%. In an embodiment, the GH10polypeptide has a sequence identity to SEQ ID NO: 102 of at least 96%.In an embodiment, the GH10 polypeptide has a sequence identity to SEQ IDNO: 102 of at least 97%. In an embodiment, the GH10 polypeptide has asequence identity to SEQ ID NO: 102 of at least 98%. In an embodiment,the GH10 polypeptide has a sequence identity to SEQ ID NO: 102 of atleast 99%.

In one embodiment, the polypeptide comprises one or more amino acidsubstitutions, and/or one or more amino acid deletions, and/or one ormore amino acid insertions or any combination thereof in between 1 and10 positions, such as 1, 2, 3, 4, 5, 6, 7, 8, 9 or 10 positions of SEQID NO: 102. In one embodiment, the polypeptide preferably comprises orconsists of the amino acid sequence of SEQ ID NO: 102 or an allelicvariant thereof; comprises SEQ ID NO: 102 or an allelic variant thereofand a N-terminal and/or C-terminal His-tag and/or HQ-tag; or is afragment thereof having xylanase activity and having at least 90% of thelength of SEQ ID NO: 102. In another embodiment, the polypeptidecomprises or consists of amino acids 1 to 337 of SEQ ID NO: 102. In anembodiment, the polypeptide has been isolated.

In an embodiment, the composition comprises a GH10 polypeptide havingxylanase activity such as the xylanase from Ustilago maydis as disclosedin Fungal Genetics and Biology 29, 145-151 (2000) and disclosed hereinas SEQ ID NO: 177. In an embodiment, the composition comprises a GH10polypeptide having xylanase activity having a sequence identity to themature polypeptide of SEQ ID NO: 176 of at least 80%, e.g., at least85%, at least 86%, at least 87%, at least 88%, at least 89%, at least90%, at least 91%, at least 92%, at least 93%, at least 94%, at least95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100%.

In one embodiment, the polypeptide comprises one or more amino acidsubstitutions, and/or one or more amino acid deletions, and/or one ormore amino acid insertions or any combination thereof in between 1 and10 positions, such as 1, 2, 3, 4, 5, 6, 7, 8, 9 or 10 positions of themature polypeptide of SEQ ID NO: 176. In one embodiment, the polypeptidepreferably comprises or consists of the amino acid sequence of SEQ IDNO: 176 or an allelic variant thereof; comprises the amino acid sequenceof SEQ ID NO: 176 and a N-terminal and/or C-terminal His-tag and/orHQ-tag such as the mature polypeptide of SEQ ID NO: 179 or SEQ ID NO:180; or is a fragment thereof having xylanase activity and having atleast 90% of the length of the mature polypeptide. In anotherembodiment, the polypeptide comprises or consists of the maturepolypeptide of SEQ ID NO: 176. In another embodiment, the polypeptidecomprises or consists of amino acids 1 to 323 of SEQ ID NO: 176. Inanother embodiment, the polypeptide comprises or consists of the maturepolypeptide of SEQ ID NO: 179. In another embodiment, the polypeptidecomprises or consists of amino acids 1 to 331 of SEQ ID NO: 179. In anembodiment, the polypeptide has been isolated.

In an embodiment, the composition comprises a GH10 polypeptide havingxylanase activity having a sequence identity to SEQ ID NO: 177 of atleast 80%. In an embodiment, the GH10 polypeptide has a sequenceidentity to SEQ ID NO: 177 of at least 85%. In an embodiment, the GH10polypeptide has a sequence identity to SEQ ID NO: 177 of at least 86%.In an embodiment, the GH10 polypeptide has a sequence identity to SEQ IDNO: 177 of at least 87%. In an embodiment, the GH10 polypeptide has asequence identity to SEQ ID NO: 177 of at least 88%. In an embodiment,the GH10 polypeptide has a sequence identity to SEQ ID NO: 177 of atleast 89%. In an embodiment, the GH10 polypeptide has a sequenceidentity to SEQ ID NO: 177 of at least 90%. In an embodiment, the GH10polypeptide has a sequence identity to SEQ ID NO: 177 of at least 91%.In an embodiment, the GH10 polypeptide has a sequence identity to SEQ IDNO: 177 of at least 92%. In an embodiment, the GH10 polypeptide has asequence identity to SEQ ID NO: 177 of at least 93%. In an embodiment,the GH10 polypeptide has a sequence identity to SEQ ID NO: 177 of atleast 94%. In an embodiment, the GH10 polypeptide has a sequenceidentity to SEQ ID NO: 177 of at least 95%. In an embodiment, the GH10polypeptide has a sequence identity to SEQ ID NO: 177 of at least 96%.In an embodiment, the GH10 polypeptide has a sequence identity to SEQ IDNO: 177 of at least 97%. In an embodiment, the GH10 polypeptide has asequence identity to SEQ ID NO: 177 of at least 98%. In an embodiment,the GH10 polypeptide has a sequence identity to SEQ ID NO: 177 of atleast 99%.

In one embodiment, the polypeptide comprises one or more amino acidsubstitutions, and/or one or more amino acid deletions, and/or one ormore amino acid insertions or any combination thereof in between 1 and10 positions, such as 1, 2, 3, 4, 5, 6, 7, 8, 9 or 10 positions of SEQID NO: 177. In one embodiment, the polypeptide comprises one or moreamino acid substitutions, and/or one or more amino acid deletions,and/or one or more amino acid insertions or any combination thereof inbetween 1 and 10 positions, such as 1, 2, 3, 4, 5, 6, 7, 8, 9 or 10positions of SEQ ID NO: 180. In one embodiment, the polypeptidepreferably comprises or consists of the amino acid sequence of SEQ IDNO: 177 or an allelic variant thereof; comprises SEQ ID NO: 177 or anallelic variant thereof and a N-terminal and/or C-terminal His-tagand/or HQ-tag such as SEQ ID NO: 180; or is a fragment thereof havingxylanase activity and having at least 90% of the length of SEQ ID NO:177. In another embodiment, the polypeptide comprises or consists ofamino acids 1 to 323 of SEQ ID NO: 177. In another embodiment, thepolypeptide comprises or consists of amino acids 1 to 331 of SEQ ID NO:180. In an embodiment, the polypeptide has been isolated.

Combinations

In the following paragraphs, specific combinations of GH10 or GH11polypeptides having xylanase activity and GH62 polypeptides havingarabinofuranosidase activity of the first aspect of the invention arelisted.

In an embodiment, the composition of the invention comprises the GH62polypeptide of SEQ ID NO: 9 and the GH10 polypeptide of SEQ ID NO: 70.In an embodiment, the composition of the invention comprises the GH62polypeptide of SEQ ID NO: 9 and the GH10 polypeptide of SEQ ID NO: 71.In an embodiment, the composition of the invention comprises the GH62polypeptide of SEQ ID NO: 9 and the GH10 polypeptide of SEQ ID NO: 72.In an embodiment, the composition of the invention comprises the GH62polypeptide of SEQ ID NO: 9 and the GH11 polypeptide of SEQ ID NO: 73.In an embodiment, the composition of the invention comprises the GH62polypeptide of SEQ ID NO: 9 and the GH11 polypeptide of SEQ ID NO: 74.In an embodiment, the composition of the invention comprises the GH62polypeptide of SEQ ID NO: 9 and the GH11 polypeptide of SEQ ID NO: 75.In an embodiment, the composition of the invention comprises the GH62polypeptide of SEQ ID NO: 9 and the GH11 polypeptide of SEQ ID NO: 78.In an embodiment, the composition of the invention comprises the GH62polypeptide of SEQ ID NO: 9 and the GH11 polypeptide of SEQ ID NO: 81.In an embodiment, the composition of the invention comprises the GH62polypeptide of SEQ ID NO: 9 and the GH11 polypeptide of SEQ ID NO: 84.In an embodiment, the composition of the invention comprises the GH62polypeptide of SEQ ID NO: 9 and the GH11 polypeptide of SEQ ID NO: 87.In an embodiment, the composition of the invention comprises the GH62polypeptide of SEQ ID NO: 9 and the GH11 polypeptide of SEQ ID NO: 88.In an embodiment, the composition of the invention comprises the GH62polypeptide of SEQ ID NO: 9 and the GH11 polypeptide of SEQ ID NO: 89.In an embodiment, the composition of the invention comprises the GH62polypeptide of SEQ ID NO: 9 and the GH10 polypeptide of SEQ ID NO: 95.In an embodiment, the composition of the invention comprises the GH62polypeptide of SEQ ID NO: 9 and the GH11 polypeptide of SEQ ID NO: 96.In an embodiment, the composition of the invention comprises the GH62polypeptide of SEQ ID NO: 9 and the GH11 polypeptide of SEQ ID NO: 99.In an embodiment, the composition of the invention comprises the GH62polypeptide of SEQ ID NO: 9 and the GH10 polypeptide of SEQ ID NO: 102.In an embodiment, the composition of the invention comprises the GH62polypeptide of SEQ ID NO: 9 and the GH10 polypeptide of SEQ ID NO: 180.

In an embodiment, the composition of the invention comprises the GH62polypeptide of SEQ ID NO: 12 and the GH10 polypeptide of SEQ ID NO: 70.In an embodiment, the composition of the invention comprises the GH62polypeptide of SEQ ID NO: 12 and the GH10 polypeptide of SEQ ID NO: 71.In an embodiment, the composition of the invention comprises the GH62polypeptide of SEQ ID NO: 12 and the GH10 polypeptide of SEQ ID NO: 72.In an embodiment, the composition of the invention comprises the GH62polypeptide of SEQ ID NO: 12 and the GH11 polypeptide of SEQ ID NO: 73.In an embodiment, the composition of the invention comprises the GH62polypeptide of SEQ ID NO: 12 and the GH11 polypeptide of SEQ ID NO: 74.In an embodiment, the composition of the invention comprises the GH62polypeptide of SEQ ID NO: 12 and the GH11 polypeptide of SEQ ID NO: 75.In an embodiment, the composition of the invention comprises the GH62polypeptide of SEQ ID NO: 12 and the GH11 polypeptide of SEQ ID NO: 78.In an embodiment, the composition of the invention comprises the GH62polypeptide of SEQ ID NO: 12 and the GH11 polypeptide of SEQ ID NO: 81.In an embodiment, the composition of the invention comprises the GH62polypeptide of SEQ ID NO: 12 and the GH11 polypeptide of SEQ ID NO: 84.In an embodiment, the composition of the invention comprises the GH62polypeptide of SEQ ID NO: 12 and the GH11 polypeptide of SEQ ID NO: 87.In an embodiment, the composition of the invention comprises the GH62polypeptide of SEQ ID NO: 12 and the GH11 polypeptide of SEQ ID NO: 88.In an embodiment, the composition of the invention comprises the GH62polypeptide of SEQ ID NO: 12 and the GH11 polypeptide of SEQ ID NO: 89.In an embodiment, the composition of the invention comprises the GH62polypeptide of SEQ ID NO: 12 and the GH10 polypeptide of SEQ ID NO: 95.In an embodiment, the composition of the invention comprises the GH62polypeptide of SEQ ID NO: 12 and the GH11 polypeptide of SEQ ID NO: 96.In an embodiment, the composition of the invention comprises the GH62polypeptide of SEQ ID NO: 12 and the GH11 polypeptide of SEQ ID NO: 99.In an embodiment, the composition of the invention comprises the GH62polypeptide of SEQ ID NO: 12 and the GH10 polypeptide of SEQ ID NO: 102.In an embodiment, the composition of the invention comprises the GH62polypeptide of SEQ ID NO: 12 and the GH10 polypeptide of SEQ ID NO: 180.

In an embodiment, the composition of the invention comprises the GH62polypeptide of SEQ ID NO: 15 and the GH10 polypeptide of SEQ ID NO: 70.In an embodiment, the composition of the invention comprises the GH62polypeptide of SEQ ID NO: 15 and the GH10 polypeptide of SEQ ID NO: 71.In an embodiment, the composition of the invention comprises the GH62polypeptide of SEQ ID NO: 15 and the GH10 polypeptide of SEQ ID NO: 72.In an embodiment, the composition of the invention comprises the GH62polypeptide of SEQ ID NO: 15 and the GH11 polypeptide of SEQ ID NO: 73.In an embodiment, the composition of the invention comprises the GH62polypeptide of SEQ ID NO: 15 and the GH11 polypeptide of SEQ ID NO: 74.In an embodiment, the composition of the invention comprises the GH62polypeptide of SEQ ID NO: 15 and the GH11 polypeptide of SEQ ID NO: 75.In an embodiment, the composition of the invention comprises the GH62polypeptide of SEQ ID NO: 15 and the GH11 polypeptide of SEQ ID NO: 78.In an embodiment, the composition of the invention comprises the GH62polypeptide of SEQ ID NO: 15 and the GH11 polypeptide of SEQ ID NO: 81.In an embodiment, the composition of the invention comprises the GH62polypeptide of SEQ ID NO: 15 and the GH11 polypeptide of SEQ ID NO: 84.In an embodiment, the composition of the invention comprises the GH62polypeptide of SEQ ID NO: 15 and the GH11 polypeptide of SEQ ID NO: 87.In an embodiment, the composition of the invention comprises the GH62polypeptide of SEQ ID NO: 15 and the GH11 polypeptide of SEQ ID NO: 88.In an embodiment, the composition of the invention comprises the GH62polypeptide of SEQ ID NO: 15 and the GH11 polypeptide of SEQ ID NO: 89.In an embodiment, the composition of the invention comprises the GH62polypeptide of SEQ ID NO: 15 and the GH10 polypeptide of SEQ ID NO: 95.In an embodiment, the composition of the invention comprises the GH62polypeptide of SEQ ID NO: 15 and the GH11 polypeptide of SEQ ID NO: 96.In an embodiment, the composition of the invention comprises the GH62polypeptide of SEQ ID NO: 15 and the GH11 polypeptide of SEQ ID NO: 99.In an embodiment, the composition of the invention comprises the GH62polypeptide of SEQ ID NO: 15 and the GH10 polypeptide of SEQ ID NO: 102.In an embodiment, the composition of the invention comprises the GH62polypeptide of SEQ ID NO: 15 and the GH10 polypeptide of SEQ ID NO: 180.

In an embodiment, the composition of the invention comprises the GH62polypeptide of SEQ ID NO: 18 and the GH10 polypeptide of SEQ ID NO: 70.In an embodiment, the composition of the invention comprises the GH62polypeptide of SEQ ID NO: 18 and the GH10 polypeptide of SEQ ID NO: 71.In an embodiment, the composition of the invention comprises the GH62polypeptide of SEQ ID NO: 18 and the GH10 polypeptide of SEQ ID NO: 72.In an embodiment, the composition of the invention comprises the GH62polypeptide of SEQ ID NO: 18 and the GH11 polypeptide of SEQ ID NO: 73.In an embodiment, the composition of the invention comprises the GH62polypeptide of SEQ ID NO: 18 and the GH11 polypeptide of SEQ ID NO: 74.In an embodiment, the composition of the invention comprises the GH62polypeptide of SEQ ID NO: 18 and the GH11 polypeptide of SEQ ID NO: 75.In an embodiment, the composition of the invention comprises the GH62polypeptide of SEQ ID NO: 18 and the GH11 polypeptide of SEQ ID NO: 78.In an embodiment, the composition of the invention comprises the GH62polypeptide of SEQ ID NO: 18 and the GH11 polypeptide of SEQ ID NO: 81.In an embodiment, the composition of the invention comprises the GH62polypeptide of SEQ ID NO: 18 and the GH11 polypeptide of SEQ ID NO: 84.In an embodiment, the composition of the invention comprises the GH62polypeptide of SEQ ID NO: 18 and the GH11 polypeptide of SEQ ID NO: 87.In an embodiment, the composition of the invention comprises the GH62polypeptide of SEQ ID NO: 18 and the GH11 polypeptide of SEQ ID NO: 88.In an embodiment, the composition of the invention comprises the GH62polypeptide of SEQ ID NO: 18 and the GH11 polypeptide of SEQ ID NO: 89.In an embodiment, the composition of the invention comprises the GH62polypeptide of SEQ ID NO: 18 and the GH10 polypeptide of SEQ ID NO: 95.In an embodiment, the composition of the invention comprises the GH62polypeptide of SEQ ID NO: 18 and the GH11 polypeptide of SEQ ID NO: 96.In an embodiment, the composition of the invention comprises the GH62polypeptide of SEQ ID NO: 18 and the GH11 polypeptide of SEQ ID NO: 99.In an embodiment, the composition of the invention comprises the GH62polypeptide of SEQ ID NO: 18 and the GH10 polypeptide of SEQ ID NO: 102.In an embodiment, the composition of the invention comprises the GH62polypeptide of SEQ ID NO: 18 and the GH10 polypeptide of SEQ ID NO: 180.

In an embodiment, the composition of the invention comprises the GH62polypeptide of SEQ ID NO: 21 and the GH10 polypeptide of SEQ ID NO: 70.In an embodiment, the composition of the invention comprises the GH62polypeptide of SEQ ID NO: 21 and the GH10 polypeptide of SEQ ID NO: 71.In an embodiment, the composition of the invention comprises the GH62polypeptide of SEQ ID NO: 21 and the GH10 polypeptide of SEQ ID NO: 72.In an embodiment, the composition of the invention comprises the GH62polypeptide of SEQ ID NO: 21 and the GH11 polypeptide of SEQ ID NO: 73.In an embodiment, the composition of the invention comprises the GH62polypeptide of SEQ ID NO: 21 and the GH11 polypeptide of SEQ ID NO: 74.In an embodiment, the composition of the invention comprises the GH62polypeptide of SEQ ID NO: 21 and the GH11 polypeptide of SEQ ID NO: 75.In an embodiment, the composition of the invention comprises the GH62polypeptide of SEQ ID NO: 21 and the GH11 polypeptide of SEQ ID NO: 78.In an embodiment, the composition of the invention comprises the GH62polypeptide of SEQ ID NO: 21 and the GH11 polypeptide of SEQ ID NO: 81.In an embodiment, the composition of the invention comprises the GH62polypeptide of SEQ ID NO: 21 and the GH11 polypeptide of SEQ ID NO: 84.In an embodiment, the composition of the invention comprises the GH62polypeptide of SEQ ID NO: 21 and the GH11 polypeptide of SEQ ID NO: 87.In an embodiment, the composition of the invention comprises the GH62polypeptide of SEQ ID NO: 21 and the GH11 polypeptide of SEQ ID NO: 88.In an embodiment, the composition of the invention comprises the GH62polypeptide of SEQ ID NO: 21 and the GH11 polypeptide of SEQ ID NO: 89.In an embodiment, the composition of the invention comprises the GH62polypeptide of SEQ ID NO: 21 and the GH10 polypeptide of SEQ ID NO: 95.In an embodiment, the composition of the invention comprises the GH62polypeptide of SEQ ID NO: 21 and the GH11 polypeptide of SEQ ID NO: 96.In an embodiment, the composition of the invention comprises the GH62polypeptide of SEQ ID NO: 21 and the GH11 polypeptide of SEQ ID NO: 99.In an embodiment, the composition of the invention comprises the GH62polypeptide of SEQ ID NO: 21 and the GH10 polypeptide of SEQ ID NO: 102.In an embodiment, the composition of the invention comprises the GH62polypeptide of SEQ ID NO: 21 and the GH10 polypeptide of SEQ ID NO: 180.

In an embodiment, the composition of the invention comprises the GH62polypeptide of SEQ ID NO: 24 and the GH10 polypeptide of SEQ ID NO: 70.In an embodiment, the composition of the invention comprises the GH62polypeptide of SEQ ID NO: 24 and the GH10 polypeptide of SEQ ID NO: 71.In an embodiment, the composition of the invention comprises the GH62polypeptide of SEQ ID NO: 24 and the GH10 polypeptide of SEQ ID NO: 72.In an embodiment, the composition of the invention comprises the GH62polypeptide of SEQ ID NO: 24 and the GH11 polypeptide of SEQ ID NO: 73.In an embodiment, the composition of the invention comprises the GH62polypeptide of SEQ ID NO: 24 and the GH11 polypeptide of SEQ ID NO: 74.In an embodiment, the composition of the invention comprises the GH62polypeptide of SEQ ID NO: 24 and the GH11 polypeptide of SEQ ID NO: 75.In an embodiment, the composition of the invention comprises the GH62polypeptide of SEQ ID NO: 24 and the GH11 polypeptide of SEQ ID NO: 78.In an embodiment, the composition of the invention comprises the GH62polypeptide of SEQ ID NO: 24 and the GH11 polypeptide of SEQ ID NO: 81.In an embodiment, the composition of the invention comprises the GH62polypeptide of SEQ ID NO: 24 and the GH11 polypeptide of SEQ ID NO: 84.In an embodiment, the composition of the invention comprises the GH62polypeptide of SEQ ID NO: 24 and the GH11 polypeptide of SEQ ID NO: 87.In an embodiment, the composition of the invention comprises the GH62polypeptide of SEQ ID NO: 24 and the GH11 polypeptide of SEQ ID NO: 88.In an embodiment, the composition of the invention comprises the GH62polypeptide of SEQ ID NO: 24 and the GH11 polypeptide of SEQ ID NO: 89.In an embodiment, the composition of the invention comprises the GH62polypeptide of SEQ ID NO: 24 and the GH10 polypeptide of SEQ ID NO: 95.In an embodiment, the composition of the invention comprises the GH62polypeptide of SEQ ID NO: 24 and the GH11 polypeptide of SEQ ID NO: 96.In an embodiment, the composition of the invention comprises the GH62polypeptide of SEQ ID NO: 24 and the GH11 polypeptide of SEQ ID NO: 99.In an embodiment, the composition of the invention comprises the GH62polypeptide of SEQ ID NO: 24 and the GH10 polypeptide of SEQ ID NO: 102.In an embodiment, the composition of the invention comprises the GH62polypeptide of SEQ ID NO: 24 and the GH10 polypeptide of SEQ ID NO: 180.

In an embodiment, the composition of the invention comprises the GH62polypeptide of SEQ ID NO: 27 and the GH10 polypeptide of SEQ ID NO: 70.In an embodiment, the composition of the invention comprises the GH62polypeptide of SEQ ID NO: 27 and the GH10 polypeptide of SEQ ID NO: 71.In an embodiment, the composition of the invention comprises the GH62polypeptide of SEQ ID NO: 27 and the GH10 polypeptide of SEQ ID NO: 72.In an embodiment, the composition of the invention comprises the GH62polypeptide of SEQ ID NO: 27 and the GH11 polypeptide of SEQ ID NO: 73.In an embodiment, the composition of the invention comprises the GH62polypeptide of SEQ ID NO: 27 and the GH11 polypeptide of SEQ ID NO: 74.In an embodiment, the composition of the invention comprises the GH62polypeptide of SEQ ID NO: 27 and the GH11 polypeptide of SEQ ID NO: 75.In an embodiment, the composition of the invention comprises the GH62polypeptide of SEQ ID NO: 27 and the GH11 polypeptide of SEQ ID NO: 78.In an embodiment, the composition of the invention comprises the GH62polypeptide of SEQ ID NO: 27 and the GH11 polypeptide of SEQ ID NO: 81.In an embodiment, the composition of the invention comprises the GH62polypeptide of SEQ ID NO: 27 and the GH11 polypeptide of SEQ ID NO: 84.In an embodiment, the composition of the invention comprises the GH62polypeptide of SEQ ID NO: 27 and the GH11 polypeptide of SEQ ID NO: 87.In an embodiment, the composition of the invention comprises the GH62polypeptide of SEQ ID NO: 27 and the GH11 polypeptide of SEQ ID NO: 88.In an embodiment, the composition of the invention comprises the GH62polypeptide of SEQ ID NO: 27 and the GH11 polypeptide of SEQ ID NO: 89.In an embodiment, the composition of the invention comprises the GH62polypeptide of SEQ ID NO: 27 and the GH10 polypeptide of SEQ ID NO: 95.In an embodiment, the composition of the invention comprises the GH62polypeptide of SEQ ID NO: 27 and the GH11 polypeptide of SEQ ID NO: 96.In an embodiment, the composition of the invention comprises the GH62polypeptide of SEQ ID NO: 27 and the GH11 polypeptide of SEQ ID NO: 99.In an embodiment, the composition of the invention comprises the GH62polypeptide of SEQ ID NO: 27 and the GH10 polypeptide of SEQ ID NO: 102.In an embodiment, the composition of the invention comprises the GH62polypeptide of SEQ ID NO: 27 and the GH10 polypeptide of SEQ ID NO: 180.

In an embodiment, the composition of the invention comprises the GH62polypeptide of SEQ ID NO: 30 and the GH10 polypeptide of SEQ ID NO: 70.In an embodiment, the composition of the invention comprises the GH62polypeptide of SEQ ID NO: 30 and the GH10 polypeptide of SEQ ID NO: 71.In an embodiment, the composition of the invention comprises the GH62polypeptide of SEQ ID NO: 30 and the GH10 polypeptide of SEQ ID NO: 72.In an embodiment, the composition of the invention comprises the GH62polypeptide of SEQ ID NO: 30 and the GH11 polypeptide of SEQ ID NO: 73.In an embodiment, the composition of the invention comprises the GH62polypeptide of SEQ ID NO: 30 and the GH11 polypeptide of SEQ ID NO: 74.In an embodiment, the composition of the invention comprises the GH62polypeptide of SEQ ID NO: 30 and the GH11 polypeptide of SEQ ID NO: 75.In an embodiment, the composition of the invention comprises the GH62polypeptide of SEQ ID NO: 30 and the GH11 polypeptide of SEQ ID NO: 78.In an embodiment, the composition of the invention comprises the GH62polypeptide of SEQ ID NO: 30 and the GH11 polypeptide of SEQ ID NO: 81.In an embodiment, the composition of the invention comprises the GH62polypeptide of SEQ ID NO: 30 and the GH11 polypeptide of SEQ ID NO: 84.In an embodiment, the composition of the invention comprises the GH62polypeptide of SEQ ID NO: 30 and the GH11 polypeptide of SEQ ID NO: 87.In an embodiment, the composition of the invention comprises the GH62polypeptide of SEQ ID NO: 30 and the GH11 polypeptide of SEQ ID NO: 88.In an embodiment, the composition of the invention comprises the GH62polypeptide of SEQ ID NO: 30 and the GH11 polypeptide of SEQ ID NO: 89.In an embodiment, the composition of the invention comprises the GH62polypeptide of SEQ ID NO: 30 and the GH10 polypeptide of SEQ ID NO: 95.In an embodiment, the composition of the invention comprises the GH62polypeptide of SEQ ID NO: 30 and the GH11 polypeptide of SEQ ID NO: 96.In an embodiment, the composition of the invention comprises the GH62polypeptide of SEQ ID NO: 30 and the GH11 polypeptide of SEQ ID NO: 99.In an embodiment, the composition of the invention comprises the GH62polypeptide of SEQ ID NO: 30 and the GH10 polypeptide of SEQ ID NO: 102.In an embodiment, the composition of the invention comprises the GH62polypeptide of SEQ ID NO: 30 and the GH10 polypeptide of SEQ ID NO: 180.

In an embodiment, the composition of the invention comprises the GH62polypeptide of SEQ ID NO: 36 and the GH10 polypeptide of SEQ ID NO: 70.In an embodiment, the composition of the invention comprises the GH62polypeptide of SEQ ID NO: 36 and the GH10 polypeptide of SEQ ID NO: 71.In an embodiment, the composition of the invention comprises the GH62polypeptide of SEQ ID NO: 36 and the GH10 polypeptide of SEQ ID NO: 72.In an embodiment, the composition of the invention comprises the GH62polypeptide of SEQ ID NO: 36 and the GH11 polypeptide of SEQ ID NO: 73.In an embodiment, the composition of the invention comprises the GH62polypeptide of SEQ ID NO: 36 and the GH11 polypeptide of SEQ ID NO: 74.In an embodiment, the composition of the invention comprises the GH62polypeptide of SEQ ID NO: 36 and the GH11 polypeptide of SEQ ID NO: 75.In an embodiment, the composition of the invention comprises the GH62polypeptide of SEQ ID NO: 36 and the GH11 polypeptide of SEQ ID NO: 78.In an embodiment, the composition of the invention comprises the GH62polypeptide of SEQ ID NO: 9 and the GH11 polypeptide of SEQ ID NO: 81.In an embodiment, the composition of the invention comprises the GH62polypeptide of SEQ ID NO: 36 and the GH11 polypeptide of SEQ ID NO: 84.In an embodiment, the composition of the invention comprises the GH62polypeptide of SEQ ID NO: 36 and the GH11 polypeptide of SEQ ID NO: 87.In an embodiment, the composition of the invention comprises the GH62polypeptide of SEQ ID NO: 36 and the GH11 polypeptide of SEQ ID NO: 88.In an embodiment, the composition of the invention comprises the GH62polypeptide of SEQ ID NO: 36 and the GH11 polypeptide of SEQ ID NO: 89.In an embodiment, the composition of the invention comprises the GH62polypeptide of SEQ ID NO: 36 and the GH10 polypeptide of SEQ ID NO: 95.In an embodiment, the composition of the invention comprises the GH62polypeptide of SEQ ID NO: 36 and the GH11 polypeptide of SEQ ID NO: 96.In an embodiment, the composition of the invention comprises the GH62polypeptide of SEQ ID NO: 36 and the GH11 polypeptide of SEQ ID NO: 99.In an embodiment, the composition of the invention comprises the GH62polypeptide of SEQ ID NO: 36 and the GH10 polypeptide of SEQ ID NO: 102.In an embodiment, the composition of the invention comprises the GH62polypeptide of SEQ ID NO: 36 and the GH10 polypeptide of SEQ ID NO: 180.

In an embodiment, the composition of the invention comprises the GH62polypeptide of SEQ ID NO: 42 and the GH10 polypeptide of SEQ ID NO: 70.In an embodiment, the composition of the invention comprises the GH62polypeptide of SEQ ID NO: 42 and the GH10 polypeptide of SEQ ID NO: 71.In an embodiment, the composition of the invention comprises the GH62polypeptide of SEQ ID NO: 42 and the GH10 polypeptide of SEQ ID NO: 72.In an embodiment, the composition of the invention comprises the GH62polypeptide of SEQ ID NO: 42 and the GH11 polypeptide of SEQ ID NO: 73.In an embodiment, the composition of the invention comprises the GH62polypeptide of SEQ ID NO: 42 and the GH11 polypeptide of SEQ ID NO: 74.In an embodiment, the composition of the invention comprises the GH62polypeptide of SEQ ID NO: 42 and the GH11 polypeptide of SEQ ID NO: 75.In an embodiment, the composition of the invention comprises the GH62polypeptide of SEQ ID NO: 42 and the GH11 polypeptide of SEQ ID NO: 78.In an embodiment, the composition of the invention comprises the GH62polypeptide of SEQ ID NO: 42 and the GH11 polypeptide of SEQ ID NO: 81.In an embodiment, the composition of the invention comprises the GH62polypeptide of SEQ ID NO: 42 and the GH11 polypeptide of SEQ ID NO: 84.In an embodiment, the composition of the invention comprises the GH62polypeptide of SEQ ID NO: 42 and the GH11 polypeptide of SEQ ID NO: 87.In an embodiment, the composition of the invention comprises the GH62polypeptide of SEQ ID NO: 42 and the GH11 polypeptide of SEQ ID NO: 88.In an embodiment, the composition of the invention comprises the GH62polypeptide of SEQ ID NO: 42 and the GH11 polypeptide of SEQ ID NO: 89.In an embodiment, the composition of the invention comprises the GH62polypeptide of SEQ ID NO: 42 and the GH10 polypeptide of SEQ ID NO: 95.In an embodiment, the composition of the invention comprises the GH62polypeptide of SEQ ID NO: 42 and the GH11 polypeptide of SEQ ID NO: 96.In an embodiment, the composition of the invention comprises the GH62polypeptide of SEQ ID NO: 42 and the GH11 polypeptide of SEQ ID NO: 99.In an embodiment, the composition of the invention comprises the GH62polypeptide of SEQ ID NO: 42 and the GH10 polypeptide of SEQ ID NO: 102.In an embodiment, the composition of the invention comprises the GH62polypeptide of SEQ ID NO: 42 and the GH10 polypeptide of SEQ ID NO: 180.

In an embodiment, the composition of the invention comprises the GH62polypeptide of SEQ ID NO: 48 and the GH10 polypeptide of SEQ ID NO: 70.In an embodiment, the composition of the invention comprises the GH62polypeptide of SEQ ID NO: 48 and the GH10 polypeptide of SEQ ID NO: 71.In an embodiment, the composition of the invention comprises the GH62polypeptide of SEQ ID NO: 48 and the GH10 polypeptide of SEQ ID NO: 72.In an embodiment, the composition of the invention comprises the GH62polypeptide of SEQ ID NO: 48 and the GH11 polypeptide of SEQ ID NO: 73.In an embodiment, the composition of the invention comprises the GH62polypeptide of SEQ ID NO: 48 and the GH11 polypeptide of SEQ ID NO: 74.In an embodiment, the composition of the invention comprises the GH62polypeptide of SEQ ID NO: 48 and the GH11 polypeptide of SEQ ID NO: 75.In an embodiment, the composition of the invention comprises the GH62polypeptide of SEQ ID NO: 48 and the GH11 polypeptide of SEQ ID NO: 78.In an embodiment, the composition of the invention comprises the GH62polypeptide of SEQ ID NO: 48 and the GH11 polypeptide of SEQ ID NO: 81.In an embodiment, the composition of the invention comprises the GH62polypeptide of SEQ ID NO: 48 and the GH11 polypeptide of SEQ ID NO: 84.In an embodiment, the composition of the invention comprises the GH62polypeptide of SEQ ID NO: 48 and the GH11 polypeptide of SEQ ID NO: 87.In an embodiment, the composition of the invention does not comprise theGH62 polypeptide of SEQ ID NO: 48 and the GH11 polypeptide of SEQ ID NO:88. In an embodiment, the composition of the invention comprises theGH62 polypeptide of SEQ ID NO: 48 and the GH11 polypeptide of SEQ ID NO:89. In an embodiment, the composition of the invention comprises theGH62 polypeptide of SEQ ID NO: 48 and the GH10 polypeptide of SEQ ID NO:95. In an embodiment, the composition of the invention comprises theGH62 polypeptide of SEQ ID NO: 48 and the GH11 polypeptide of SEQ ID NO:96. In an embodiment, the composition of the invention comprises theGH62 polypeptide of SEQ ID NO: 48 and the GH11 polypeptide of SEQ ID NO:99. In an embodiment, the composition of the invention comprises theGH62 polypeptide of SEQ ID NO: 48 and the GH10 polypeptide of SEQ ID NO:102. In an embodiment, the composition of the invention comprises theGH62 polypeptide of SEQ ID NO: 48 and the GH10 polypeptide of SEQ ID NO:180.

In an embodiment, the composition of the invention comprises the GH62polypeptide of SEQ ID NO: 54 and the GH10 polypeptide of SEQ ID NO: 70.In an embodiment, the composition of the invention comprises the GH62polypeptide of SEQ ID NO: 54 and the GH10 polypeptide of SEQ ID NO: 71.In an embodiment, the composition of the invention comprises the GH62polypeptide of SEQ ID NO: 54 and the GH10 polypeptide of SEQ ID NO: 72.In an embodiment, the composition of the invention comprises the GH62polypeptide of SEQ ID NO: 54 and the GH11 polypeptide of SEQ ID NO: 73.In an embodiment, the composition of the invention comprises the GH62polypeptide of SEQ ID NO: 54 and the GH11 polypeptide of SEQ ID NO: 74.In an embodiment, the composition of the invention comprises the GH62polypeptide of SEQ ID NO: 54 and the GH11 polypeptide of SEQ ID NO: 75.In an embodiment, the composition of the invention comprises the GH62polypeptide of SEQ ID NO: 54 and the GH11 polypeptide of SEQ ID NO: 78.In an embodiment, the composition of the invention comprises the GH62polypeptide of SEQ ID NO: 54 and the GH11 polypeptide of SEQ ID NO: 81.In an embodiment, the composition of the invention comprises the GH62polypeptide of SEQ ID NO: 54 and the GH11 polypeptide of SEQ ID NO: 84.In an embodiment, the composition of the invention comprises the GH62polypeptide of SEQ ID NO: 54 and the GH11 polypeptide of SEQ ID NO: 87.In an embodiment, the composition of the invention comprises the GH62polypeptide of SEQ ID NO: 54 and the GH11 polypeptide of SEQ ID NO: 88.In an embodiment, the composition of the invention comprises the GH62polypeptide of SEQ ID NO: 54 and the GH11 polypeptide of SEQ ID NO: 89.In an embodiment, the composition of the invention comprises the GH62polypeptide of SEQ ID NO: 54 and the GH10 polypeptide of SEQ ID NO: 95.In an embodiment, the composition of the invention comprises the GH62polypeptide of SEQ ID NO: 54 and the GH11 polypeptide of SEQ ID NO: 96.In an embodiment, the composition of the invention comprises the GH62polypeptide of SEQ ID NO: 54 and the GH11 polypeptide of SEQ ID NO: 99.In an embodiment, the composition of the invention comprises the GH62polypeptide of SEQ ID NO: 54 and the GH10 polypeptide of SEQ ID NO: 102.In an embodiment, the composition of the invention comprises the GH62polypeptide of SEQ ID NO: 54 and the GH10 polypeptide of SEQ ID NO: 180.

In an embodiment, the composition of the invention comprises the GH62polypeptide of SEQ ID NO: 60 and the GH10 polypeptide of SEQ ID NO: 70.In an embodiment, the composition of the invention comprises the GH62polypeptide of SEQ ID NO: 60 and the GH10 polypeptide of SEQ ID NO: 71.In an embodiment, the composition of the invention comprises the GH62polypeptide of SEQ ID NO: 60 and the GH10 polypeptide of SEQ ID NO: 72.In an embodiment, the composition of the invention comprises the GH62polypeptide of SEQ ID NO: 60 and the GH11 polypeptide of SEQ ID NO: 73.In an embodiment, the composition of the invention comprises the GH62polypeptide of SEQ ID NO: 60 and the GH11 polypeptide of SEQ ID NO: 74.In an embodiment, the composition of the invention comprises the GH62polypeptide of SEQ ID NO: 60 and the GH11 polypeptide of SEQ ID NO: 75.In an embodiment, the composition of the invention comprises the GH62polypeptide of SEQ ID NO: 60 and the GH11 polypeptide of SEQ ID NO: 78.In an embodiment, the composition of the invention comprises the GH62polypeptide of SEQ ID NO: 60 and the GH11 polypeptide of SEQ ID NO: 81.In an embodiment, the composition of the invention comprises the GH62polypeptide of SEQ ID NO: 60 and the GH11 polypeptide of SEQ ID NO: 84.In an embodiment, the composition of the invention comprises the GH62polypeptide of SEQ ID NO: 60 and the GH11 polypeptide of SEQ ID NO: 87.In an embodiment, the composition of the invention comprises the GH62polypeptide of SEQ ID NO: 60 and the GH11 polypeptide of SEQ ID NO: 88.In an embodiment, the composition of the invention comprises the GH62polypeptide of SEQ ID NO: 60 and the GH11 polypeptide of SEQ ID NO: 89.In an embodiment, the composition of the invention comprises the GH62polypeptide of SEQ ID NO: 60 and the GH10 polypeptide of SEQ ID NO: 95.In an embodiment, the composition of the invention comprises the GH62polypeptide of SEQ ID NO: 60 and the GH11 polypeptide of SEQ ID NO: 96.In an embodiment, the composition of the invention comprises the GH62polypeptide of SEQ ID NO: 60 and the GH11 polypeptide of SEQ ID NO: 99.In an embodiment, the composition of the invention comprises the GH62polypeptide of SEQ ID NO: 60 and the GH10 polypeptide of SEQ ID NO: 102.In an embodiment, the composition of the invention comprises the GH62polypeptide of SEQ ID NO: 60 and the GH10 polypeptide of SEQ ID NO: 180.

In an embodiment, the composition of the invention comprises the GH62polypeptide of SEQ ID NO: 66 and the GH10 polypeptide of SEQ ID NO: 70.In an embodiment, the composition of the invention comprises the GH62polypeptide of SEQ ID NO: 66 and the GH10 polypeptide of SEQ ID NO: 71.In an embodiment, the composition of the invention comprises the GH62polypeptide of SEQ ID NO: 66 and the GH10 polypeptide of SEQ ID NO: 72.In an embodiment, the composition of the invention comprises the GH62polypeptide of SEQ ID NO: 66 and the GH11 polypeptide of SEQ ID NO: 73.In an embodiment, the composition of the invention comprises the GH62polypeptide of SEQ ID NO: 66 and the GH11 polypeptide of SEQ ID NO: 74.In an embodiment, the composition of the invention comprises the GH62polypeptide of SEQ ID NO: 66 and the GH11 polypeptide of SEQ ID NO: 75.In an embodiment, the composition of the invention comprises the GH62polypeptide of SEQ ID NO: 66 and the GH11 polypeptide of SEQ ID NO: 78.In an embodiment, the composition of the invention comprises the GH62polypeptide of SEQ ID NO: 66 and the GH11 polypeptide of SEQ ID NO: 81.In an embodiment, the composition of the invention comprises the GH62polypeptide of SEQ ID NO: 66 and the GH11 polypeptide of SEQ ID NO: 84.In an embodiment, the composition of the invention comprises the GH62polypeptide of SEQ ID NO: 66 and the GH11 polypeptide of SEQ ID NO: 87.In an embodiment, the composition of the invention comprises the GH62polypeptide of SEQ ID NO: 66 and the GH11 polypeptide of SEQ ID NO: 88.In an embodiment, the composition of the invention comprises the GH62polypeptide of SEQ ID NO: 66 and the GH11 polypeptide of SEQ ID NO: 89.In an embodiment, the composition of the invention comprises the GH62polypeptide of SEQ ID NO: 66 and the GH10 polypeptide of SEQ ID NO: 95.In an embodiment, the composition of the invention comprises the GH62polypeptide of SEQ ID NO: 66 and the GH11 polypeptide of SEQ ID NO: 96.In an embodiment, the composition of the invention comprises the GH62polypeptide of SEQ ID NO: 66 and the GH11 polypeptide of SEQ ID NO: 99.In an embodiment, the composition of the invention comprises the GH62polypeptide of SEQ ID NO: 66 and the GH10 polypeptide of SEQ ID NO: 102.In an embodiment, the composition of the invention comprises the GH62polypeptide of SEQ ID NO: 66 and the GH10 polypeptide of SEQ ID NO: 180.

In an embodiment, the composition of the invention comprises the GH62polypeptide of SEQ ID NO: 105 and the GH10 polypeptide of SEQ ID NO: 70.In an embodiment, the composition of the invention comprises the GH62polypeptide of SEQ ID NO: 105 and the GH10 polypeptide of SEQ ID NO: 71.In an embodiment, the composition of the invention comprises the GH62polypeptide of SEQ ID NO: 105 and the GH10 polypeptide of SEQ ID NO: 72.In an embodiment, the composition of the invention comprises the GH62polypeptide of SEQ ID NO: 105 and the GH11 polypeptide of SEQ ID NO: 73.In an embodiment, the composition of the invention comprises the GH62polypeptide of SEQ ID NO: 105 and the GH11 polypeptide of SEQ ID NO: 74.In an embodiment, the composition of the invention comprises the GH62polypeptide of SEQ ID NO: 105 and the GH11 polypeptide of SEQ ID NO: 75.In an embodiment, the composition of the invention comprises the GH62polypeptide of SEQ ID NO: 105 and the GH11 polypeptide of SEQ ID NO: 78.In an embodiment, the composition of the invention comprises the GH62polypeptide of SEQ ID NO: 105 and the GH11 polypeptide of SEQ ID NO: 81.In an embodiment, the composition of the invention comprises the GH62polypeptide of SEQ ID NO: 105 and the GH11 polypeptide of SEQ ID NO: 84.In an embodiment, the composition of the invention comprises the GH62polypeptide of SEQ ID NO: 105 and the GH11 polypeptide of SEQ ID NO: 87.In an embodiment, the composition of the invention comprises the GH62polypeptide of SEQ ID NO: 105 and the GH11 polypeptide of SEQ ID NO: 88.In an embodiment, the composition of the invention comprises the GH62polypeptide of SEQ ID NO: 105 and the GH11 polypeptide of SEQ ID NO: 89.In an embodiment, the composition of the invention comprises the GH62polypeptide of SEQ ID NO: 105 and the GH10 polypeptide of SEQ ID NO: 95.In an embodiment, the composition of the invention comprises the GH62polypeptide of SEQ ID NO: 105 and the GH11 polypeptide of SEQ ID NO: 96.In an embodiment, the composition of the invention comprises the GH62polypeptide of SEQ ID NO: 105 and the GH11 polypeptide of SEQ ID NO: 99.In an embodiment, the composition of the invention comprises the GH62polypeptide of SEQ ID NO: 105 and the GH10 polypeptide of SEQ ID NO:102. In an embodiment, the composition of the invention comprises theGH62 polypeptide of SEQ ID NO: 105 and the GH10 polypeptide of SEQ IDNO: 180.

In an embodiment, the composition of the invention comprises the GH62polypeptide of SEQ ID NO: 108 and the GH10 polypeptide of SEQ ID NO: 70.In an embodiment, the composition of the invention comprises the GH62polypeptide of SEQ ID NO: 108 and the GH10 polypeptide of SEQ ID NO: 71.In an embodiment, the composition of the invention comprises the GH62polypeptide of SEQ ID NO: 108 and the GH10 polypeptide of SEQ ID NO: 72.In an embodiment, the composition of the invention comprises the GH62polypeptide of SEQ ID NO: 108 and the GH11 polypeptide of SEQ ID NO: 73.In an embodiment, the composition of the invention comprises the GH62polypeptide of SEQ ID NO: 108 and the GH11 polypeptide of SEQ ID NO: 74.In an embodiment, the composition of the invention comprises the GH62polypeptide of SEQ ID NO: 108 and the GH11 polypeptide of SEQ ID NO: 75.In an embodiment, the composition of the invention comprises the GH62polypeptide of SEQ ID NO: 108 and the GH11 polypeptide of SEQ ID NO: 78.In an embodiment, the composition of the invention comprises the GH62polypeptide of SEQ ID NO: 108 and the GH11 polypeptide of SEQ ID NO: 81.In an embodiment, the composition of the invention comprises the GH62polypeptide of SEQ ID NO: 108 and the GH11 polypeptide of SEQ ID NO: 84.In an embodiment, the composition of the invention comprises the GH62polypeptide of SEQ ID NO: 108 and the GH11 polypeptide of SEQ ID NO: 87.In an embodiment, the composition of the invention comprises the GH62polypeptide of SEQ ID NO: 108 and the GH11 polypeptide of SEQ ID NO: 88.In an embodiment, the composition of the invention comprises the GH62polypeptide of SEQ ID NO: 108 and the GH11 polypeptide of SEQ ID NO: 89.In an embodiment, the composition of the invention comprises the GH62polypeptide of SEQ ID NO: 108 and the GH10 polypeptide of SEQ ID NO: 95.In an embodiment, the composition of the invention comprises the GH62polypeptide of SEQ ID NO: 108 and the GH11 polypeptide of SEQ ID NO: 96.In an embodiment, the composition of the invention comprises the GH62polypeptide of SEQ ID NO: 108 and the GH11 polypeptide of SEQ ID NO: 99.In an embodiment, the composition of the invention comprises the GH62polypeptide of SEQ ID NO: 108 and the GH10 polypeptide of SEQ ID NO:102. In an embodiment, the composition of the invention comprises theGH62 polypeptide of SEQ ID NO: 108 and the GH10 polypeptide of SEQ IDNO: 180.

In an embodiment, the composition of the invention comprises the GH62polypeptide of SEQ ID NO: 114 and the GH10 polypeptide of SEQ ID NO: 70.In an embodiment, the composition of the invention comprises the GH62polypeptide of SEQ ID NO: 114 and the GH10 polypeptide of SEQ ID NO: 71.In an embodiment, the composition of the invention comprises the GH62polypeptide of SEQ ID NO: 114 and the GH10 polypeptide of SEQ ID NO: 72.In an embodiment, the composition of the invention comprises the GH62polypeptide of SEQ ID NO: 114 and the GH11 polypeptide of SEQ ID NO: 73.In an embodiment, the composition of the invention comprises the GH62polypeptide of SEQ ID NO: 114 and the GH11 polypeptide of SEQ ID NO: 74.In an embodiment, the composition of the invention comprises the GH62polypeptide of SEQ ID NO: 114 and the GH11 polypeptide of SEQ ID NO: 75.In an embodiment, the composition of the invention comprises the GH62polypeptide of SEQ ID NO: 114 and the GH11 polypeptide of SEQ ID NO: 78.In an embodiment, the composition of the invention comprises the GH62polypeptide of SEQ ID NO: 114 and the GH11 polypeptide of SEQ ID NO: 81.In an embodiment, the composition of the invention comprises the GH62polypeptide of SEQ ID NO: 114 and the GH11 polypeptide of SEQ ID NO: 84.In an embodiment, the composition of the invention comprises the GH62polypeptide of SEQ ID NO: 114 and the GH11 polypeptide of SEQ ID NO: 87.In an embodiment, the composition of the invention comprises the GH62polypeptide of SEQ ID NO: 114 and the GH11 polypeptide of SEQ ID NO: 88.In an embodiment, the composition of the invention comprises the GH62polypeptide of SEQ ID NO: 114 and the GH11 polypeptide of SEQ ID NO: 89.In an embodiment, the composition of the invention comprises the GH62polypeptide of SEQ ID NO: 114 and the GH10 polypeptide of SEQ ID NO: 95.In an embodiment, the composition of the invention comprises the GH62polypeptide of SEQ ID NO: 114 and the GH11 polypeptide of SEQ ID NO: 96.In an embodiment, the composition of the invention comprises the GH62polypeptide of SEQ ID NO: 114 and the GH11 polypeptide of SEQ ID NO: 99.In an embodiment, the composition of the invention comprises the GH62polypeptide of SEQ ID NO: 114 and the GH10 polypeptide of SEQ ID NO:102. In an embodiment, the composition of the invention comprises theGH62 polypeptide of SEQ ID NO: 114 and the GH10 polypeptide of SEQ IDNO: 180.

In an embodiment, the composition of the invention comprises the GH62polypeptide of SEQ ID NO: 120 and the GH10 polypeptide of SEQ ID NO: 70.In an embodiment, the composition of the invention comprises the GH62polypeptide of SEQ ID NO: 120 and the GH10 polypeptide of SEQ ID NO: 71.In an embodiment, the composition of the invention comprises the GH62polypeptide of SEQ ID NO: 120 and the GH10 polypeptide of SEQ ID NO: 72.In an embodiment, the composition of the invention comprises the GH62polypeptide of SEQ ID NO: 120 and the GH11 polypeptide of SEQ ID NO: 73.In an embodiment, the composition of the invention comprises the GH62polypeptide of SEQ ID NO: 120 and the GH11 polypeptide of SEQ ID NO: 74.In an embodiment, the composition of the invention comprises the GH62polypeptide of SEQ ID NO: 120 and the GH11 polypeptide of SEQ ID NO: 75.In an embodiment, the composition of the invention comprises the GH62polypeptide of SEQ ID NO: 120 and the GH11 polypeptide of SEQ ID NO: 78.In an embodiment, the composition of the invention comprises the GH62polypeptide of SEQ ID NO: 120 and the GH11 polypeptide of SEQ ID NO: 81.In an embodiment, the composition of the invention comprises the GH62polypeptide of SEQ ID NO: 120 and the GH11 polypeptide of SEQ ID NO: 84.In an embodiment, the composition of the invention comprises the GH62polypeptide of SEQ ID NO: 120 and the GH11 polypeptide of SEQ ID NO: 87.In an embodiment, the composition of the invention comprises the GH62polypeptide of SEQ ID NO: 120 and the GH11 polypeptide of SEQ ID NO: 88.In an embodiment, the composition of the invention comprises the GH62polypeptide of SEQ ID NO: 120 and the GH11 polypeptide of SEQ ID NO: 89.In an embodiment, the composition of the invention comprises the GH62polypeptide of SEQ ID NO: 120 and the GH10 polypeptide of SEQ ID NO: 95.In an embodiment, the composition of the invention comprises the GH62polypeptide of SEQ ID NO: 120 and the GH11 polypeptide of SEQ ID NO: 96.In an embodiment, the composition of the invention comprises the GH62polypeptide of SEQ ID NO: 120 and the GH11 polypeptide of SEQ ID NO: 99.In an embodiment, the composition of the invention comprises the GH62polypeptide of SEQ ID NO: 120 and the GH10 polypeptide of SEQ ID NO:102. In an embodiment, the composition of the invention comprises theGH62 polypeptide of SEQ ID NO: 120 and the GH10 polypeptide of SEQ IDNO: 180.

In an embodiment, the composition of the invention comprises the GH62polypeptide of SEQ ID NO: 123 and the GH10 polypeptide of SEQ ID NO: 70.In an embodiment, the composition of the invention comprises the GH62polypeptide of SEQ ID NO: 123 and the GH10 polypeptide of SEQ ID NO: 71.In an embodiment, the composition of the invention comprises the GH62polypeptide of SEQ ID NO: 123 and the GH10 polypeptide of SEQ ID NO: 72.In an embodiment, the composition of the invention comprises the GH62polypeptide of SEQ ID NO: 123 and the GH11 polypeptide of SEQ ID NO: 73.In an embodiment, the composition of the invention comprises the GH62polypeptide of SEQ ID NO: 123 and the GH11 polypeptide of SEQ ID NO: 74.In an embodiment, the composition of the invention comprises the GH62polypeptide of SEQ ID NO: 123 and the GH11 polypeptide of SEQ ID NO: 75.In an embodiment, the composition of the invention comprises the GH62polypeptide of SEQ ID NO: 123 and the GH11 polypeptide of SEQ ID NO: 78.In an embodiment, the composition of the invention comprises the GH62polypeptide of SEQ ID NO: 123 and the GH11 polypeptide of SEQ ID NO: 81.In an embodiment, the composition of the invention comprises the GH62polypeptide of SEQ ID NO: 123 and the GH11 polypeptide of SEQ ID NO: 84.In an embodiment, the composition of the invention comprises the GH62polypeptide of SEQ ID NO: 123 and the GH11 polypeptide of SEQ ID NO: 87.In an embodiment, the composition of the invention comprises the GH62polypeptide of SEQ ID NO: 123 and the GH11 polypeptide of SEQ ID NO: 88.In an embodiment, the composition of the invention comprises the GH62polypeptide of SEQ ID NO: 123 and the GH11 polypeptide of SEQ ID NO: 89.In an embodiment, the composition of the invention comprises the GH62polypeptide of SEQ ID NO: 123 and the GH10 polypeptide of SEQ ID NO: 95.In an embodiment, the composition of the invention comprises the GH62polypeptide of SEQ ID NO: 123 and the GH11 polypeptide of SEQ ID NO: 96.In an embodiment, the composition of the invention comprises the GH62polypeptide of SEQ ID NO: 123 and the GH11 polypeptide of SEQ ID NO: 99.In an embodiment, the composition of the invention comprises the GH62polypeptide of SEQ ID NO: 123 and the GH10 polypeptide of SEQ ID NO:102. In an embodiment, the composition of the invention comprises theGH62 polypeptide of SEQ ID NO: 123 and the GH10 polypeptide of SEQ IDNO: 180.

In an embodiment, the composition of the invention comprises the GH62polypeptide of SEQ ID NO: 126 and the GH10 polypeptide of SEQ ID NO: 70.In an embodiment, the composition of the invention comprises the GH62polypeptide of SEQ ID NO: 126 and the GH10 polypeptide of SEQ ID NO: 71.In an embodiment, the composition of the invention comprises the GH62polypeptide of SEQ ID NO: 126 and the GH10 polypeptide of SEQ ID NO: 72.In an embodiment, the composition of the invention comprises the GH62polypeptide of SEQ ID NO: 126 and the GH11 polypeptide of SEQ ID NO: 73.In an embodiment, the composition of the invention comprises the GH62polypeptide of SEQ ID NO: 126 and the GH11 polypeptide of SEQ ID NO: 74.In an embodiment, the composition of the invention comprises the GH62polypeptide of SEQ ID NO: 126 and the GH11 polypeptide of SEQ ID NO: 75.In an embodiment, the composition of the invention comprises the GH62polypeptide of SEQ ID NO: 126 and the GH11 polypeptide of SEQ ID NO: 78.In an embodiment, the composition of the invention comprises the GH62polypeptide of SEQ ID NO: 126 and the GH11 polypeptide of SEQ ID NO: 81.In an embodiment, the composition of the invention comprises the GH62polypeptide of SEQ ID NO: 126 and the GH11 polypeptide of SEQ ID NO: 84.In an embodiment, the composition of the invention comprises the GH62polypeptide of SEQ ID NO: 126 and the GH11 polypeptide of SEQ ID NO: 87.In an embodiment, the composition of the invention comprises the GH62polypeptide of SEQ ID NO: 126 and the GH11 polypeptide of SEQ ID NO: 88.In an embodiment, the composition of the invention comprises the GH62polypeptide of SEQ ID NO: 126 and the GH11 polypeptide of SEQ ID NO: 89.In an embodiment, the composition of the invention comprises the GH62polypeptide of SEQ ID NO: 126 and the GH10 polypeptide of SEQ ID NO: 95.In an embodiment, the composition of the invention comprises the GH62polypeptide of SEQ ID NO: 126 and the GH11 polypeptide of SEQ ID NO: 96.In an embodiment, the composition of the invention comprises the GH62polypeptide of SEQ ID NO: 126 and the GH11 polypeptide of SEQ ID NO: 99.In an embodiment, the composition of the invention comprises the GH62polypeptide of SEQ ID NO: 126 and the GH10 polypeptide of SEQ ID NO:102. In an embodiment, the composition of the invention comprises theGH62 polypeptide of SEQ ID NO: 126 and the GH10 polypeptide of SEQ IDNO: 180.

In an embodiment, the composition of the invention comprises the GH62polypeptide of SEQ ID NO: 132 and the GH10 polypeptide of SEQ ID NO: 70.In an embodiment, the composition of the invention comprises the GH62polypeptide of SEQ ID NO: 132 and the GH10 polypeptide of SEQ ID NO: 71.In an embodiment, the composition of the invention comprises the GH62polypeptide of SEQ ID NO: 132 and the GH10 polypeptide of SEQ ID NO: 72.In an embodiment, the composition of the invention comprises the GH62polypeptide of SEQ ID NO: 132 and the GH11 polypeptide of SEQ ID NO: 73.In an embodiment, the composition of the invention comprises the GH62polypeptide of SEQ ID NO: 132 and the GH11 polypeptide of SEQ ID NO: 74.In an embodiment, the composition of the invention comprises the GH62polypeptide of SEQ ID NO: 132 and the GH11 polypeptide of SEQ ID NO: 75.In an embodiment, the composition of the invention comprises the GH62polypeptide of SEQ ID NO: 132 and the GH11 polypeptide of SEQ ID NO: 78.In an embodiment, the composition of the invention comprises the GH62polypeptide of SEQ ID NO: 132 and the GH11 polypeptide of SEQ ID NO: 81.In an embodiment, the composition of the invention comprises the GH62polypeptide of SEQ ID NO: 132 and the GH11 polypeptide of SEQ ID NO: 84.In an embodiment, the composition of the invention comprises the GH62polypeptide of SEQ ID NO: 132 and the GH11 polypeptide of SEQ ID NO: 87.In an embodiment, the composition of the invention comprises the GH62polypeptide of SEQ ID NO: 132 and the GH11 polypeptide of SEQ ID NO: 88.In an embodiment, the composition of the invention comprises the GH62polypeptide of SEQ ID NO: 132 and the GH11 polypeptide of SEQ ID NO: 89.In an embodiment, the composition of the invention comprises the GH62polypeptide of SEQ ID NO: 132 and the GH10 polypeptide of SEQ ID NO: 95.In an embodiment, the composition of the invention comprises the GH62polypeptide of SEQ ID NO: 132 and the GH11 polypeptide of SEQ ID NO: 96.In an embodiment, the composition of the invention comprises the GH62polypeptide of SEQ ID NO: 132 and the GH11 polypeptide of SEQ ID NO: 99.In an embodiment, the composition of the invention comprises the GH62polypeptide of SEQ ID NO: 132 and the GH10 polypeptide of SEQ ID NO:102. In an embodiment, the composition of the invention comprises theGH62 polypeptide of SEQ ID NO: 132 and the GH10 polypeptide of SEQ IDNO: 180.

In an embodiment, the composition of the invention comprises the GH62polypeptide of SEQ ID NO: 138 and the GH10 polypeptide of SEQ ID NO: 70.In an embodiment, the composition of the invention comprises the GH62polypeptide of SEQ ID NO: 138 and the GH10 polypeptide of SEQ ID NO: 71.In an embodiment, the composition of the invention comprises the GH62polypeptide of SEQ ID NO: 138 and the GH10 polypeptide of SEQ ID NO: 72.In an embodiment, the composition of the invention comprises the GH62polypeptide of SEQ ID NO: 138 and the GH11 polypeptide of SEQ ID NO: 73.In an embodiment, the composition of the invention comprises the GH62polypeptide of SEQ ID NO: 138 and the GH11 polypeptide of SEQ ID NO: 74.In an embodiment, the composition of the invention comprises the GH62polypeptide of SEQ ID NO: 138 and the GH11 polypeptide of SEQ ID NO: 75.In an embodiment, the composition of the invention comprises the GH62polypeptide of SEQ ID NO: 138 and the GH11 polypeptide of SEQ ID NO: 78.In an embodiment, the composition of the invention comprises the GH62polypeptide of SEQ ID NO: 138 and the GH11 polypeptide of SEQ ID NO: 81.In an embodiment, the composition of the invention comprises the GH62polypeptide of SEQ ID NO: 138 and the GH11 polypeptide of SEQ ID NO: 84.In an embodiment, the composition of the invention comprises the GH62polypeptide of SEQ ID NO: 138 and the GH11 polypeptide of SEQ ID NO: 87.In an embodiment, the composition of the invention comprises the GH62polypeptide of SEQ ID NO: 138 and the GH11 polypeptide of SEQ ID NO: 88.In an embodiment, the composition of the invention comprises the GH62polypeptide of SEQ ID NO: 138 and the GH11 polypeptide of SEQ ID NO: 89.In an embodiment, the composition of the invention comprises the GH62polypeptide of SEQ ID NO: 138 and the GH10 polypeptide of SEQ ID NO: 95.In an embodiment, the composition of the invention comprises the GH62polypeptide of SEQ ID NO: 138 and the GH11 polypeptide of SEQ ID NO: 96.In an embodiment, the composition of the invention comprises the GH62polypeptide of SEQ ID NO: 138 and the GH11 polypeptide of SEQ ID NO: 99.In an embodiment, the composition of the invention comprises the GH62polypeptide of SEQ ID NO: 138 and the GH10 polypeptide of SEQ ID NO:102. In an embodiment, the composition of the invention comprises theGH62 polypeptide of SEQ ID NO: 138 and the GH10 polypeptide of SEQ IDNO: 180.

In an embodiment, the composition of the invention comprises the GH62polypeptide of SEQ ID NO: 141 and the GH10 polypeptide of SEQ ID NO: 70.In an embodiment, the composition of the invention comprises the GH62polypeptide of SEQ ID NO: 141 and the GH10 polypeptide of SEQ ID NO: 71.In an embodiment, the composition of the invention comprises the GH62polypeptide of SEQ ID NO: 141 and the GH10 polypeptide of SEQ ID NO: 72.In an embodiment, the composition of the invention comprises the GH62polypeptide of SEQ ID NO: 141 and the GH11 polypeptide of SEQ ID NO: 73.In an embodiment, the composition of the invention comprises the GH62polypeptide of SEQ ID NO: 141 and the GH11 polypeptide of SEQ ID NO: 74.In an embodiment, the composition of the invention comprises the GH62polypeptide of SEQ ID NO: 141 and the GH11 polypeptide of SEQ ID NO: 75.In an embodiment, the composition of the invention comprises the GH62polypeptide of SEQ ID NO: 141 and the GH11 polypeptide of SEQ ID NO: 78.In an embodiment, the composition of the invention comprises the GH62polypeptide of SEQ ID NO: 141 and the GH11 polypeptide of SEQ ID NO: 81.In an embodiment, the composition of the invention comprises the GH62polypeptide of SEQ ID NO: 141 and the GH11 polypeptide of SEQ ID NO: 84.In an embodiment, the composition of the invention comprises the GH62polypeptide of SEQ ID NO: 141 and the GH11 polypeptide of SEQ ID NO: 87.In an embodiment, the composition of the invention comprises the GH62polypeptide of SEQ ID NO: 141 and the GH11 polypeptide of SEQ ID NO: 88.In an embodiment, the composition of the invention comprises the GH62polypeptide of SEQ ID NO: 141 and the GH11 polypeptide of SEQ ID NO: 89.In an embodiment, the composition of the invention comprises the GH62polypeptide of SEQ ID NO: 141 and the GH10 polypeptide of SEQ ID NO: 95.In an embodiment, the composition of the invention comprises the GH62polypeptide of SEQ ID NO: 141 and the GH11 polypeptide of SEQ ID NO: 96.In an embodiment, the composition of the invention comprises the GH62polypeptide of SEQ ID NO: 141 and the GH11 polypeptide of SEQ ID NO: 99.In an embodiment, the composition of the invention comprises the GH62polypeptide of SEQ ID NO: 141 and the GH10 polypeptide of SEQ ID NO:102. In an embodiment, the composition of the invention comprises theGH62 polypeptide of SEQ ID NO: 141 and the GH10 polypeptide of SEQ IDNO: 180.

In an embodiment, the composition of the invention comprises the GH62polypeptide of SEQ ID NO: 147 and the GH10 polypeptide of SEQ ID NO: 70.In an embodiment, the composition of the invention comprises the GH62polypeptide of SEQ ID NO: 147 and the GH10 polypeptide of SEQ ID NO: 71.In an embodiment, the composition of the invention comprises the GH62polypeptide of SEQ ID NO: 147 and the GH10 polypeptide of SEQ ID NO: 72.In an embodiment, the composition of the invention comprises the GH62polypeptide of SEQ ID NO: 147 and the GH11 polypeptide of SEQ ID NO: 73.In an embodiment, the composition of the invention comprises the GH62polypeptide of SEQ ID NO: 147 and the GH11 polypeptide of SEQ ID NO: 74.In an embodiment, the composition of the invention comprises the GH62polypeptide of SEQ ID NO: 147 and the GH11 polypeptide of SEQ ID NO: 75.In an embodiment, the composition of the invention comprises the GH62polypeptide of SEQ ID NO: 147 and the GH11 polypeptide of SEQ ID NO: 78.In an embodiment, the composition of the invention comprises the GH62polypeptide of SEQ ID NO: 147 and the GH11 polypeptide of SEQ ID NO: 81.In an embodiment, the composition of the invention comprises the GH62polypeptide of SEQ ID NO: 147 and the GH11 polypeptide of SEQ ID NO: 84.In an embodiment, the composition of the invention comprises the GH62polypeptide of SEQ ID NO: 147 and the GH11 polypeptide of SEQ ID NO: 87.In an embodiment, the composition of the invention comprises the GH62polypeptide of SEQ ID NO: 147 and the GH11 polypeptide of SEQ ID NO: 88.In an embodiment, the composition of the invention comprises the GH62polypeptide of SEQ ID NO: 147 and the GH11 polypeptide of SEQ ID NO: 89.In an embodiment, the composition of the invention comprises the GH62polypeptide of SEQ ID NO: 147 and the GH10 polypeptide of SEQ ID NO: 95.In an embodiment, the composition of the invention comprises the GH62polypeptide of SEQ ID NO: 147 and the GH11 polypeptide of SEQ ID NO: 96.In an embodiment, the composition of the invention comprises the GH62polypeptide of SEQ ID NO: 147 and the GH11 polypeptide of SEQ ID NO: 99.In an embodiment, the composition of the invention comprises the GH62polypeptide of SEQ ID NO: 147 and the GH10 polypeptide of SEQ ID NO:102. In an embodiment, the composition of the invention comprises theGH62 polypeptide of SEQ ID NO: 147 and the GH10 polypeptide of SEQ IDNO: 180.

In an embodiment, the composition of the invention comprises the GH62polypeptide of SEQ ID NO: 150 and the GH10 polypeptide of SEQ ID NO: 70.In an embodiment, the composition of the invention comprises the GH62polypeptide of SEQ ID NO: 150 and the GH10 polypeptide of SEQ ID NO: 71.In an embodiment, the composition of the invention comprises the GH62polypeptide of SEQ ID NO: 150 and the GH10 polypeptide of SEQ ID NO: 72.In an embodiment, the composition of the invention comprises the GH62polypeptide of SEQ ID NO: 150 and the GH11 polypeptide of SEQ ID NO: 73.In an embodiment, the composition of the invention comprises the GH62polypeptide of SEQ ID NO: 150 and the GH11 polypeptide of SEQ ID NO: 74.In an embodiment, the composition of the invention comprises the GH62polypeptide of SEQ ID NO: 150 and the GH11 polypeptide of SEQ ID NO: 75.In an embodiment, the composition of the invention comprises the GH62polypeptide of SEQ ID NO: 150 and the GH11 polypeptide of SEQ ID NO: 78.In an embodiment, the composition of the invention comprises the GH62polypeptide of SEQ ID NO: 150 and the GH11 polypeptide of SEQ ID NO: 81.In an embodiment, the composition of the invention comprises the GH62polypeptide of SEQ ID NO: 150 and the GH11 polypeptide of SEQ ID NO: 84.In an embodiment, the composition of the invention comprises the GH62polypeptide of SEQ ID NO: 150 and the GH11 polypeptide of SEQ ID NO: 87.In an embodiment, the composition of the invention comprises the GH62polypeptide of SEQ ID NO: 150 and the GH11 polypeptide of SEQ ID NO: 88.In an embodiment, the composition of the invention comprises the GH62polypeptide of SEQ ID NO: 150 and the GH11 polypeptide of SEQ ID NO: 89.In an embodiment, the composition of the invention comprises the GH62polypeptide of SEQ ID NO: 150 and the GH10 polypeptide of SEQ ID NO: 95.In an embodiment, the composition of the invention comprises the GH62polypeptide of SEQ ID NO: 150 and the GH11 polypeptide of SEQ ID NO: 96.In an embodiment, the composition of the invention comprises the GH62polypeptide of SEQ ID NO: 150 and the GH11 polypeptide of SEQ ID NO: 99.In an embodiment, the composition of the invention comprises the GH62polypeptide of SEQ ID NO: 150 and the GH10 polypeptide of SEQ ID NO:102. In an embodiment, the composition of the invention comprises theGH62 polypeptide of SEQ ID NO: 150 and the GH10 polypeptide of SEQ IDNO: 180.

In an embodiment, the composition of the invention comprises the GH62polypeptide of SEQ ID NO: 156 and the GH10 polypeptide of SEQ ID NO: 70.In an embodiment, the composition of the invention comprises the GH62polypeptide of SEQ ID NO: 156 and the GH10 polypeptide of SEQ ID NO: 71.In an embodiment, the composition of the invention comprises the GH62polypeptide of SEQ ID NO: 156 and the GH10 polypeptide of SEQ ID NO: 72.In an embodiment, the composition of the invention comprises the GH62polypeptide of SEQ ID NO: 156 and the GH11 polypeptide of SEQ ID NO: 73.In an embodiment, the composition of the invention comprises the GH62polypeptide of SEQ ID NO: 156 and the GH11 polypeptide of SEQ ID NO: 74.In an embodiment, the composition of the invention comprises the GH62polypeptide of SEQ ID NO: 156 and the GH11 polypeptide of SEQ ID NO: 75.In an embodiment, the composition of the invention comprises the GH62polypeptide of SEQ ID NO: 156 and the GH11 polypeptide of SEQ ID NO: 78.In an embodiment, the composition of the invention comprises the GH62polypeptide of SEQ ID NO: 156 and the GH11 polypeptide of SEQ ID NO: 81.In an embodiment, the composition of the invention comprises the GH62polypeptide of SEQ ID NO: 156 and the GH11 polypeptide of SEQ ID NO: 84.In an embodiment, the composition of the invention comprises the GH62polypeptide of SEQ ID NO: 156 and the GH11 polypeptide of SEQ ID NO: 87.In an embodiment, the composition of the invention comprises the GH62polypeptide of SEQ ID NO: 156 and the GH11 polypeptide of SEQ ID NO: 88.In an embodiment, the composition of the invention comprises the GH62polypeptide of SEQ ID NO: 156 and the GH11 polypeptide of SEQ ID NO: 89.In an embodiment, the composition of the invention comprises the GH62polypeptide of SEQ ID NO: 156 and the GH10 polypeptide of SEQ ID NO: 95.In an embodiment, the composition of the invention comprises the GH62polypeptide of SEQ ID NO: 156 and the GH11 polypeptide of SEQ ID NO: 96.In an embodiment, the composition of the invention comprises the GH62polypeptide of SEQ ID NO: 156 and the GH11 polypeptide of SEQ ID NO: 99.In an embodiment, the composition of the invention comprises the GH62polypeptide of SEQ ID NO: 156 and the GH10 polypeptide of SEQ ID NO:102. In an embodiment, the composition of the invention comprises theGH62 polypeptide of SEQ ID NO: 156 and the GH10 polypeptide of SEQ IDNO: 180.

In an embodiment, the composition of the invention comprises the GH62polypeptide of SEQ ID NO: 159 and the GH10 polypeptide of SEQ ID NO: 70.In an embodiment, the composition of the invention comprises the GH62polypeptide of SEQ ID NO: 159 and the GH10 polypeptide of SEQ ID NO: 71.In an embodiment, the composition of the invention comprises the GH62polypeptide of SEQ ID NO: 159 and the GH10 polypeptide of SEQ ID NO: 72.In an embodiment, the composition of the invention comprises the GH62polypeptide of SEQ ID NO: 159 and the GH11 polypeptide of SEQ ID NO: 73.In an embodiment, the composition of the invention comprises the GH62polypeptide of SEQ ID NO: 159 and the GH11 polypeptide of SEQ ID NO: 74.In an embodiment, the composition of the invention comprises the GH62polypeptide of SEQ ID NO: 159 and the GH11 polypeptide of SEQ ID NO: 75.In an embodiment, the composition of the invention comprises the GH62polypeptide of SEQ ID NO: 159 and the GH11 polypeptide of SEQ ID NO: 78.In an embodiment, the composition of the invention comprises the GH62polypeptide of SEQ ID NO: 159 and the GH11 polypeptide of SEQ ID NO: 81.In an embodiment, the composition of the invention comprises the GH62polypeptide of SEQ ID NO: 159 and the GH11 polypeptide of SEQ ID NO: 84.In an embodiment, the composition of the invention comprises the GH62polypeptide of SEQ ID NO: 159 and the GH11 polypeptide of SEQ ID NO: 87.In an embodiment, the composition of the invention comprises the GH62polypeptide of SEQ ID NO: 159 and the GH11 polypeptide of SEQ ID NO: 88.In an embodiment, the composition of the invention comprises the GH62polypeptide of SEQ ID NO: 159 and the GH11 polypeptide of SEQ ID NO: 89.In an embodiment, the composition of the invention comprises the GH62polypeptide of SEQ ID NO: 159 and the GH10 polypeptide of SEQ ID NO: 95.In an embodiment, the composition of the invention comprises the GH62polypeptide of SEQ ID NO: 159 and the GH11 polypeptide of SEQ ID NO: 96.In an embodiment, the composition of the invention comprises the GH62polypeptide of SEQ ID NO: 159 and the GH11 polypeptide of SEQ ID NO: 99.In an embodiment, the composition of the invention comprises the GH62polypeptide of SEQ ID NO: 159 and the GH10 polypeptide of SEQ ID NO:102. In an embodiment, the composition of the invention comprises theGH62 polypeptide of SEQ ID NO: 159 and the GH10 polypeptide of SEQ IDNO: 180.

In an embodiment, the composition of the invention comprises the GH62polypeptide of SEQ ID NO: 162 and the GH10 polypeptide of SEQ ID NO: 70.In an embodiment, the composition of the invention comprises the GH62polypeptide of SEQ ID NO: 162 and the GH10 polypeptide of SEQ ID NO: 71.In an embodiment, the composition of the invention comprises the GH62polypeptide of SEQ ID NO: 162 and the GH10 polypeptide of SEQ ID NO: 72.In an embodiment, the composition of the invention comprises the GH62polypeptide of SEQ ID NO: 162 and the GH11 polypeptide of SEQ ID NO: 73.In an embodiment, the composition of the invention comprises the GH62polypeptide of SEQ ID NO: 162 and the GH11 polypeptide of SEQ ID NO: 74.In an embodiment, the composition of the invention comprises the GH62polypeptide of SEQ ID NO: 162 and the GH11 polypeptide of SEQ ID NO: 75.In an embodiment, the composition of the invention comprises the GH62polypeptide of SEQ ID NO: 162 and the GH11 polypeptide of SEQ ID NO: 78.In an embodiment, the composition of the invention comprises the GH62polypeptide of SEQ ID NO: 162 and the GH11 polypeptide of SEQ ID NO: 81.In an embodiment, the composition of the invention comprises the GH62polypeptide of SEQ ID NO: 162 and the GH11 polypeptide of SEQ ID NO: 84.In an embodiment, the composition of the invention comprises the GH62polypeptide of SEQ ID NO: 162 and the GH11 polypeptide of SEQ ID NO: 87.In an embodiment, the composition of the invention comprises the GH62polypeptide of SEQ ID NO: 162 and the GH11 polypeptide of SEQ ID NO: 88.In an embodiment, the composition of the invention comprises the GH62polypeptide of SEQ ID NO: 162 and the GH11 polypeptide of SEQ ID NO: 89.In an embodiment, the composition of the invention comprises the GH62polypeptide of SEQ ID NO: 162 and the GH10 polypeptide of SEQ ID NO: 95.In an embodiment, the composition of the invention comprises the GH62polypeptide of SEQ ID NO: 162 and the GH11 polypeptide of SEQ ID NO: 96.In an embodiment, the composition of the invention comprises the GH62polypeptide of SEQ ID NO: 162 and the GH11 polypeptide of SEQ ID NO: 99.In an embodiment, the composition of the invention comprises the GH62polypeptide of SEQ ID NO: 162 and the GH10 polypeptide of SEQ ID NO:102. In an embodiment, the composition of the invention comprises theGH62 polypeptide of SEQ ID NO: 162 and the GH10 polypeptide of SEQ IDNO: 180.

In an embodiment, the composition of the invention comprises the GH62polypeptide of SEQ ID NO: 165 and the GH10 polypeptide of SEQ ID NO: 70.In an embodiment, the composition of the invention comprises the GH62polypeptide of SEQ ID NO: 165 and the GH10 polypeptide of SEQ ID NO: 71.In an embodiment, the composition of the invention comprises the GH62polypeptide of SEQ ID NO: 165 and the GH10 polypeptide of SEQ ID NO: 72.In an embodiment, the composition of the invention comprises the GH62polypeptide of SEQ ID NO: 165 and the GH11 polypeptide of SEQ ID NO: 73.In an embodiment, the composition of the invention comprises the GH62polypeptide of SEQ ID NO: 165 and the GH11 polypeptide of SEQ ID NO: 74.In an embodiment, the composition of the invention comprises the GH62polypeptide of SEQ ID NO: 165 and the GH11 polypeptide of SEQ ID NO: 75.In an embodiment, the composition of the invention comprises the GH62polypeptide of SEQ ID NO: 165 and the GH11 polypeptide of SEQ ID NO: 78.In an embodiment, the composition of the invention comprises the GH62polypeptide of SEQ ID NO: 165 and the GH11 polypeptide of SEQ ID NO: 81.In an embodiment, the composition of the invention comprises the GH62polypeptide of SEQ ID NO: 165 and the GH11 polypeptide of SEQ ID NO: 84.In an embodiment, the composition of the invention comprises the GH62polypeptide of SEQ ID NO: 165 and the GH11 polypeptide of SEQ ID NO: 87.In an embodiment, the composition of the invention comprises the GH62polypeptide of SEQ ID NO: 165 and the GH11 polypeptide of SEQ ID NO: 88.In an embodiment, the composition of the invention comprises the GH62polypeptide of SEQ ID NO: 165 and the GH11 polypeptide of SEQ ID NO: 89.In an embodiment, the composition of the invention comprises the GH62polypeptide of SEQ ID NO: 165 and the GH10 polypeptide of SEQ ID NO: 95.In an embodiment, the composition of the invention comprises the GH62polypeptide of SEQ ID NO: 165 and the GH11 polypeptide of SEQ ID NO: 96.In an embodiment, the composition of the invention comprises the GH62polypeptide of SEQ ID NO: 165 and the GH11 polypeptide of SEQ ID NO: 99.In an embodiment, the composition of the invention comprises the GH62polypeptide of SEQ ID NO: 165 and the GH10 polypeptide of SEQ ID NO:102. In an embodiment, the composition of the invention comprises theGH62 polypeptide of SEQ ID NO: 165 and the GH10 polypeptide of SEQ IDNO: 180.

In an embodiment, the composition of the invention comprises the GH62polypeptide of SEQ ID NO: 168 and the GH10 polypeptide of SEQ ID NO: 70.In an embodiment, the composition of the invention comprises the GH62polypeptide of SEQ ID NO: 168 and the GH10 polypeptide of SEQ ID NO: 71.In an embodiment, the composition of the invention comprises the GH62polypeptide of SEQ ID NO: 168 and the GH10 polypeptide of SEQ ID NO: 72.In an embodiment, the composition of the invention comprises the GH62polypeptide of SEQ ID NO: 168 and the GH11 polypeptide of SEQ ID NO: 73.In an embodiment, the composition of the invention comprises the GH62polypeptide of SEQ ID NO: 168 and the GH11 polypeptide of SEQ ID NO: 74.In an embodiment, the composition of the invention comprises the GH62polypeptide of SEQ ID NO: 168 and the GH11 polypeptide of SEQ ID NO: 75.In an embodiment, the composition of the invention comprises the GH62polypeptide of SEQ ID NO: 168 and the GH11 polypeptide of SEQ ID NO: 78.In an embodiment, the composition of the invention comprises the GH62polypeptide of SEQ ID NO: 168 and the GH11 polypeptide of SEQ ID NO: 81.In an embodiment, the composition of the invention comprises the GH62polypeptide of SEQ ID NO: 168 and the GH11 polypeptide of SEQ ID NO: 84.In an embodiment, the composition of the invention comprises the GH62polypeptide of SEQ ID NO: 168 and the GH11 polypeptide of SEQ ID NO: 87.In an embodiment, the composition of the invention comprises the GH62polypeptide of SEQ ID NO: 168 and the GH11 polypeptide of SEQ ID NO: 88.In an embodiment, the composition of the invention comprises the GH62polypeptide of SEQ ID NO: 168 and the GH11 polypeptide of SEQ ID NO: 89.In an embodiment, the composition of the invention comprises the GH62polypeptide of SEQ ID NO: 168 and the GH10 polypeptide of SEQ ID NO: 95.In an embodiment, the composition of the invention comprises the GH62polypeptide of SEQ ID NO: 168 and the GH11 polypeptide of SEQ ID NO: 96.In an embodiment, the composition of the invention comprises the GH62polypeptide of SEQ ID NO: 168 and the GH11 polypeptide of SEQ ID NO: 99.In an embodiment, the composition of the invention comprises the GH62polypeptide of SEQ ID NO: 168 and the GH10 polypeptide of SEQ ID NO:102. In an embodiment, the composition of the invention comprises theGH62 polypeptide of SEQ ID NO: 168 and the GH10 polypeptide of SEQ IDNO: 180.

In an embodiment, the composition of the invention comprises the GH62polypeptide of SEQ ID NO: 171 and the GH10 polypeptide of SEQ ID NO: 70.In an embodiment, the composition of the invention comprises the GH62polypeptide of SEQ ID NO: 171 and the GH10 polypeptide of SEQ ID NO: 71.In an embodiment, the composition of the invention comprises the GH62polypeptide of SEQ ID NO: 171 and the GH10 polypeptide of SEQ ID NO: 72.In an embodiment, the composition of the invention comprises the GH62polypeptide of SEQ ID NO: 171 and the GH11 polypeptide of SEQ ID NO: 73.In an embodiment, the composition of the invention comprises the GH62polypeptide of SEQ ID NO: 171 and the GH11 polypeptide of SEQ ID NO: 74.In an embodiment, the composition of the invention comprises the GH62polypeptide of SEQ ID NO: 171 and the GH11 polypeptide of SEQ ID NO: 75.In an embodiment, the composition of the invention comprises the GH62polypeptide of SEQ ID NO: 171 and the GH11 polypeptide of SEQ ID NO: 78.In an embodiment, the composition of the invention comprises the GH62polypeptide of SEQ ID NO: 171 and the GH11 polypeptide of SEQ ID NO: 81.In an embodiment, the composition of the invention comprises the GH62polypeptide of SEQ ID NO: 171 and the GH11 polypeptide of SEQ ID NO: 84.In an embodiment, the composition of the invention comprises the GH62polypeptide of SEQ ID NO: 171 and the GH11 polypeptide of SEQ ID NO: 87.In an embodiment, the composition of the invention comprises the GH62polypeptide of SEQ ID NO: 171 and the GH11 polypeptide of SEQ ID NO: 88.In an embodiment, the composition of the invention comprises the GH62polypeptide of SEQ ID NO: 171 and the GH11 polypeptide of SEQ ID NO: 89.In an embodiment, the composition of the invention comprises the GH62polypeptide of SEQ ID NO: 171 and the GH10 polypeptide of SEQ ID NO: 95.In an embodiment, the composition of the invention comprises the GH62polypeptide of SEQ ID NO: 171 and the GH11 polypeptide of SEQ ID NO: 96.In an embodiment, the composition of the invention comprises the GH62polypeptide of SEQ ID NO: 171 and the GH11 polypeptide of SEQ ID NO: 99.In an embodiment, the composition of the invention comprises the GH62polypeptide of SEQ ID NO: 171 and the GH10 polypeptide of SEQ ID NO:102. In an embodiment, the composition of the invention comprises theGH62 polypeptide of SEQ ID NO: 171 and the GH10 polypeptide of SEQ IDNO: 180.

In an embodiment, the composition of the invention comprises the GH62polypeptide of SEQ ID NO: 174 and the GH10 polypeptide of SEQ ID NO: 70.In an embodiment, the composition of the invention comprises the GH62polypeptide of SEQ ID NO: 174 and the GH10 polypeptide of SEQ ID NO: 71.In an embodiment, the composition of the invention comprises the GH62polypeptide of SEQ ID NO: 174 and the GH10 polypeptide of SEQ ID NO: 72.In an embodiment, the composition of the invention comprises the GH62polypeptide of SEQ ID NO: 174 and the GH11 polypeptide of SEQ ID NO: 73.In an embodiment, the composition of the invention comprises the GH62polypeptide of SEQ ID NO: 174 and the GH11 polypeptide of SEQ ID NO: 74.In an embodiment, the composition of the invention comprises the GH62polypeptide of SEQ ID NO: 174 and the GH11 polypeptide of SEQ ID NO: 75.In an embodiment, the composition of the invention comprises the GH62polypeptide of SEQ ID NO: 174 and the GH11 polypeptide of SEQ ID NO: 78.In an embodiment, the composition of the invention comprises the GH62polypeptide of SEQ ID NO: 174 and the GH11 polypeptide of SEQ ID NO: 81.In an embodiment, the composition of the invention comprises the GH62polypeptide of SEQ ID NO: 174 and the GH11 polypeptide of SEQ ID NO: 84.In an embodiment, the composition of the invention comprises the GH62polypeptide of SEQ ID NO: 174 and the GH11 polypeptide of SEQ ID NO: 87.In an embodiment, the composition of the invention comprises the GH62polypeptide of SEQ ID NO: 174 and the GH11 polypeptide of SEQ ID NO: 88.In an embodiment, the composition of the invention comprises the GH62polypeptide of SEQ ID NO: 174 and the GH11 polypeptide of SEQ ID NO: 89.In an embodiment, the composition of the invention comprises the GH62polypeptide of SEQ ID NO: 174 and the GH10 polypeptide of SEQ ID NO: 95.In an embodiment, the composition of the invention comprises the GH62polypeptide of SEQ ID NO: 174 and the GH11 polypeptide of SEQ ID NO: 96.In an embodiment, the composition of the invention comprises the GH62polypeptide of SEQ ID NO: 174 and the GH11 polypeptide of SEQ ID NO: 99.In an embodiment, the composition of the invention comprises the GH62polypeptide of SEQ ID NO: 174 and the GH10 polypeptide of SEQ ID NO:102. In an embodiment, the composition of the invention comprises theGH62 polypeptide of SEQ ID NO: 174 and the GH10 polypeptide of SEQ IDNO: 180.

In a further preferred embodiment, the composition of the inventioncomprises one or more GH10 polypeptides selected from the listconsisting of SEQ ID NO: 71, SEQ ID NO: 72 and SEQ ID NO: 180 and one ormore GH62 polypeptides selected from the list consisting of SEQ ID NO:9, SEQ ID NO: 21, SEQ ID NO: 24, SEQ ID NO: 27, SEQ ID NO: 45, SEQ IDNO: 51, SEQ ID NO: 57, SEQ ID NO: 69, SEQ ID NO: 105, SEQ ID NO: 123,SEQ ID NO: 129, SEQ ID NO: 138, SEQ ID NO: 147, SEQ ID NO: 153, SEQ IDNO: 156, SEQ ID NO: 159, SEQ ID NO: 162, SEQ ID NO: 165, SEQ ID NO: 171and SEQ ID NO: 174.

In a further preferred embodiment, the animal feed or animal feedadditive of the invention comprises one or more GH10 polypeptidesselected from the list consisting of SEQ ID NO: 71, SEQ ID NO: 72 andSEQ ID NO: 180 and one or more GH62 polypeptides selected from the listconsisting of SEQ ID NO: 9, SEQ ID NO: 21, SEQ ID NO: 24, SEQ ID NO: 27,SEQ ID NO: 45, SEQ ID NO: 51, SEQ ID NO: 57, SEQ ID NO: 69, SEQ ID NO:105, SEQ ID NO: 123, SEQ ID NO: 129, SEQ ID NO: 138, SEQ ID NO: 147, SEQID NO: 153, SEQ ID NO: 156, SEQ ID NO: 159, SEQ ID NO: 162, SEQ ID NO:165, SEQ ID NO: 171 and SEQ ID NO: 174. In an embodiment, the GH10polypeptide is dosed at 0.01-200 mg enzyme protein per kg animal feedand the GH62 polypeptide is dosed at 0.01-200 mg enzyme protein per kganimal feed.

In a further preferred embodiment, the composition of the inventioncomprises the GH11 polypeptide of SEQ ID NO: 73 and one or more GH62polypeptides selected from the list consisting of SEQ ID NO: 24, SEQ IDNO: 33, SEQ ID NO: 39, SEQ ID NO: 45, SEQ ID NO: 51, SEQ ID NO: 69, SEQID NO: 105, SEQ ID NO: 111, SEQ ID NO: 117, SEQ ID NO: 123, SEQ ID NO:129, SEQ ID NO: 138, SEQ ID NO: 144, SEQ ID NO: 147, SEQ ID NO: 153, SEQID NO: 156, SEQ ID NO: 159, SEQ ID NO: 162, SEQ ID NO: 165, SEQ ID NO:171 and SEQ ID NO: 174.

In a further preferred embodiment, the animal feed or animal feedadditive of the invention comprises the GH11 polypeptide of SEQ ID NO:73 and one or more GH62 polypeptides selected from the list consistingof SEQ ID NO: 24, SEQ ID NO: 33, SEQ ID NO: 39, SEQ ID NO: 45, SEQ IDNO: 51, SEQ ID NO: 69, SEQ ID NO: 105, SEQ ID NO: 111, SEQ ID NO: 117,SEQ ID NO: 123, SEQ ID NO: 129, SEQ ID NO: 138, SEQ ID NO: 144, SEQ IDNO: 147, SEQ ID NO: 153, SEQ ID NO: 156, SEQ ID NO: 159, SEQ ID NO: 162,SEQ ID NO: 165, SEQ ID NO: 171 and SEQ ID NO: 174. In an embodiment, theGH10 polypeptide is dosed at 0.01-200 mg enzyme protein per kg animalfeed and the GH62 polypeptide is dosed at 0.01-200 mg enzyme protein perkg animal feed.

In a further preferred embodiment, the composition of the inventioncomprises one or more GH11 polypeptides selected from the listconsisting of SEQ ID NO: 75, SEQ ID NO: 78, SEQ ID NO: 81, SEQ ID NO:87, SEQ ID NO: 88, SEQ ID NO: 96 and SEQ ID NO: 99 and one or more GH62polypeptides selected from the list consisting of SEQ ID NO: 21, SEQ IDNO: 24, SEQ ID NO: 27, SEQ ID NO: 33, SEQ ID NO: 39, SEQ ID NO: 45, SEQID NO: 51, SEQ ID NO: 57, SEQ ID NO: 63, SEQ ID NO: 69, SEQ ID NO: 105,SEQ ID NO: 111, SEQ ID NO: 117, SEQ ID NO: 123, SEQ ID NO: 129, SEQ IDNO: 138, SEQ ID NO: 144, SEQ ID NO: 147, SEQ ID NO: 153, SEQ ID NO: 156,SEQ ID NO: 159, SEQ ID NO: 162, SEQ ID NO: 165, SEQ ID NO: 171 and SEQID NO: 174.

In a further preferred embodiment, the animal feed or animal feedadditive of the invention comprises one or more GH11 polypeptidesselected from the list consisting of SEQ ID NO: 75, SEQ ID NO: 78, SEQID NO: 81, SEQ ID NO: 87, SEQ ID NO: 88, SEQ ID NO: 96 and SEQ ID NO: 99and one or more GH62 polypeptides selected from the list consisting ofSEQ ID NO: 21, SEQ ID NO: 24, SEQ ID NO: 27, SEQ ID NO: 33, SEQ ID NO:39, SEQ ID NO: 45, SEQ ID NO: 51, SEQ ID NO: 57, SEQ ID NO: 63, SEQ IDNO: 69, SEQ ID NO: 105, SEQ ID NO: 111, SEQ ID NO: 117, SEQ ID NO: 123,SEQ ID NO: 129, SEQ ID NO: 138, SEQ ID NO: 144, SEQ ID NO: 147, SEQ IDNO: 153, SEQ ID NO: 156, SEQ ID NO: 159, SEQ ID NO: 162, SEQ ID NO: 165,SEQ ID NO: 171 and SEQ ID NO: 174. In an embodiment, the GH10polypeptide is dosed at 0.01-200 mg enzyme protein per kg animal feedand the GH62 polypeptide is dosed at 0.01-200 mg enzyme protein per kganimal feed.

In a further embodiment, the specific combinations of GH10 or GH11polypeptides having xylanase activity and GH62 polypeptides havingarabinofuranosidase activity as listed above solubilises at least 2.0%,such as at least 2.5%, at least 3.0%, at least 3.5%, at least 4.0%, atleast 4.5%, at least 5.0%, at least 5.5%, or at least 6.0% xylose fromDFDSM and solubilises at least 2 times more xylose from DFDSM than theGH10 or GH11 polypeptide can when the GH62 polypeptide is not present.

In a further embodiment, the specific combinations of GH10 or GH11polypeptides having xylanase activity and GH62 polypeptides havingarabinofuranosidase activity as listed above solubilises at least 2.0%,such as at least 2.5%, at least 3.0%, at least 3.5%, at least 4.0%, atleast 4.5%, at least 5.0%, at least 5.5%, or at least 6.0% xylose fromDFDSM and solubilises at least 2.25 times more xylose from DFDSM thanthe GH10 or GH11 polypeptide can when the GH62 polypeptide is notpresent.

In a further embodiment, the specific combinations of GH10 or GH11polypeptides having xylanase activity and GH62 polypeptides havingarabinofuranosidase activity as listed above solubilises at least 2.0%,such as at least 2.5%, at least 3.0%, at least 3.5%, at least 4.0%, atleast 4.5%, at least 5.0%, at least 5.5%, or at least 6.0% xylose fromDFDSM and solubilises at least 2.5 times more xylose from DFDSM than theGH10 or GH11 polypeptide can when the GH62 polypeptide is not present.

In a further embodiment, the specific combinations of GH10 or GH11polypeptides having xylanase activity and GH62 polypeptides havingarabinofuranosidase activity as listed above solubilises at least 2.0%,such as at least 2.5%, at least 3.0%, at least 3.5%, at least 4.0%, atleast 4.5%, at least 5.0%, at least 5.5%, or at least 6.0% xylose fromDFDSM and solubilises at least 2.75 times more xylose from DFDSM thanthe GH10 or GH11 polypeptide can when the GH62 polypeptide is notpresent.

In a further embodiment, the specific combinations of GH10 or GH11polypeptides having xylanase activity and GH62 polypeptides havingarabinofuranosidase activity as listed above solubilises at least 2.0%,such as at least 2.5%, at least 3.0%, at least 3.5%, at least 4.0%, atleast 4.5%, at least 5.0%, at least 5.5%, or at least 6.0% xylose fromDFDSM and solubilises at least 3 times more xylose from DFDSM than theGH10 or GH11 polypeptide can when the GH62 polypeptide is not present.

In a further embodiment, the specific combinations of GH10 or GH11polypeptides having xylanase activity and GH62 polypeptides havingarabinofuranosidase activity as listed above solubilises at least 2.0%,such as at least 2.5%, at least 3.0%, at least 3.5%, at least 4.0%, atleast 4.5%, at least 5.0%, at least 5.5%, or at least 6.0% xylose fromDFDSM and solubilises at least 3.25 times more xylose from DFDSM thanthe GH10 or GH11 polypeptide can when the GH62 polypeptide is notpresent.

In a further embodiment, the specific combinations of GH10 or GH11polypeptides having xylanase activity and GH62 polypeptides havingarabinofuranosidase activity as listed above solubilises at least 2.0%,such as at least 2.5%, at least 3.0%, at least 3.5%, at least 4.0%, atleast 4.5%, at least 5.0%, at least 5.5%, or at least 6.0% xylose fromDFDSM and solubilises at least 3.5 times more xylose from DFDSM than theGH10 or GH11 polypeptide can when the GH62 polypeptide is not present.

In a further embodiment, the specific combinations of GH10 or GH11polypeptides having xylanase activity and GH62 polypeptides havingarabinofuranosidase activity as listed above solubilises at least 2.0%,such as at least 2.5%, at least 3.0%, at least 3.5%, at least 4.0%, atleast 4.5%, at least 5.0%, at least 5.5%, or at least 6.0% xylose fromDFDSM and solubilises at least 3.75 times more xylose from DFDSM thanthe GH10 or GH11 polypeptide can when the GH62 polypeptide is notpresent.

In a further embodiment, the specific combinations of GH10 or GH11polypeptides having xylanase activity and GH62 polypeptides havingarabinofuranosidase activity as listed above solubilises at least 2.0%,such as at least 2.5%, at least 3.0%, at least 3.5%, at least 4.0%, atleast 4.5%, at least 5.0%, at least 5.5%, or at least 6.0% xylose fromDFDSM and solubilises at least 4 times more xylose from DFDSM than theGH10 or GH11 polypeptide can when the GH62 polypeptide is not present.

Polypeptides Having Arabinofuranosidase Activity

In a second aspect, the invention relates to polypeptides havingarabinofuranosidase activity and having a sequence identity to themature polypeptide of SEQ ID NO: 11 of at least 85%, e.g., at least 86%,at least 87%, at least 88%, at least 89%, at least 90%, at least 91%, atleast 92%, at least 93%, at least 94%, at least 95%, at least 96%, atleast 97%, at least 98%, at least 99%, which have arabinofuranosidaseactivity. In one embodiment, the polypeptides differ by up to 45 aminoacids, e.g., between 1 and 45 amino acids, such as 1-40, 1-35, 1-30,1-25, 1-20, 1-15, 1-10 or 1-5 amino acids, or 1, 2, 3, 4, 5, 6, 7, 8, 9,10, 11, 12, 13, 14, 15, 16, 17, 18, 19, 20, 21, 22, 23, 24, 25, 26, 27,28, 29, 30, 31, 32, 33, 34, 35, 36, 37, 38, 39, 40, 41, 42, 43, 44 or 45amino acids from the mature polypeptide of SEQ ID NO: 11.

In a continuation of the second aspect, the invention further relates topolypeptides having a sequence identity to SEQ ID NO: 12 of at least 85%which have arabinofuranosidase activity. In an embodiment, thepolypeptide has a sequence identity to SEQ ID NO: 12 of at least 86%. Inan embodiment, the polypeptide has a sequence identity to SEQ ID NO: 12of at least 87%. In an embodiment, the polypeptide has a sequenceidentity to SEQ ID NO: 12 of at least 88%. In an embodiment, thepolypeptide has a sequence identity to SEQ ID NO: 12 of at least 89%. Inan embodiment, the polypeptide has a sequence identity to SEQ ID NO: 12of at least 90%. In an embodiment, the polypeptide has a sequenceidentity to SEQ ID NO: 12 of at least 91%. In an embodiment, thepolypeptide has a sequence identity to SEQ ID NO: 12 of at least 92%. Inan embodiment, the polypeptide has a sequence identity to SEQ ID NO: 12of at least 93%. In an embodiment, the polypeptide has a sequenceidentity to SEQ ID NO: 12 of at least 94%. In an embodiment, thepolypeptide has a sequence identity to SEQ ID NO: 12 of at least 95%. Inan embodiment, the polypeptide has a sequence identity to SEQ ID NO: 12of at least 96%. In an embodiment, the polypeptide has a sequenceidentity to SEQ ID NO: 12 of at least 97%. In an embodiment, thepolypeptide has a sequence identity to SEQ ID NO: 12 of at least 98%. Inan embodiment, the polypeptide has a sequence identity to SEQ ID NO: 12of at least 99%.

In one embodiment, the polypeptides differ by up to 45 amino acids,e.g., between 1 and 50 amino acids, such as 1-40, 1-35, 1-30, 1-25,1-20, 1-15, 1-10 or 1-5 amino acids, or 1, 2, 3, 4, 5, 6, 7, 8, 9, 10,11, 12, 13, 14, 15, 16, 17, 18, 19, 20, 21, 22, 23, 24, 25, 26, 27, 28,29, 30, 31, 32, 33, 34, 35, 36, 37, 38, 39, 40, 41, 42, 43, 44 or 45amino acids from SEQ ID NO: 12. In an embodiment, the polypeptide has atleast 60%, at least 70%, at least 75%, at least 80%, at least 85%, atleast 90%, at least 95%, or at least 100% of the activity of thepolypeptide of SEQ ID NO: 12.

In one embodiment, the polypeptide preferably comprises or consists ofthe amino acid sequence of SEQ ID NO: 11 and/or SEQ ID NO: 12 or anallelic variant thereof; comprises the amino acid sequence of SEQ ID NO:11 and/or SEQ ID NO: 12 and a N-terminal and/or C-terminal His-tagand/or HQ-tag; or is a fragment thereof having arabinofuranosidaseactivity and having at least 90% such as at least 91%, at least 92%, atleast 93%, at least 94%, at least 95%, at least 96%, at least 97%, atleast 98% or at least 99% of the length of the mature polypeptide. Inanother embodiment, the polypeptide comprises or consists of the maturepolypeptide of SEQ ID NO: 12. In another embodiment, the polypeptidecomprises or consists of amino acids 1 to 303 of SEQ ID NO: 11. Inanother embodiment, the polypeptide comprises or consists of amino acids1 to 303 of SEQ ID NO: 12. In an embodiment, the polypeptide has beenisolated.

In a continuation of the second aspect, the invention relates to apolypeptide having arabinofuranosidase activity encoded by apolynucleotide that hybridizes under high stringency conditions or veryhigh stringency conditions with (i) the mature polypeptide codingsequence of SEQ ID NO: 10 or (ii) the full-length complement of (i).(Sambrook et al., 1989, Molecular Cloning, A Laboratory Manual, 2dedition, Cold Spring Harbor, N.Y.). In an embodiment, the polypeptidehas been isolated.

In a continuation of the second aspect, the invention relates to apolypeptide having arabinofuranosidase activity encoded by apolynucleotide having a sequence identity to the mature polypeptidecoding sequence of SEQ ID NO: 10 or the cDNA sequence thereof of atleast 85%, e.g., at least 86%, at least 87%, at least 88%, at least 89%,at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, atleast 95%, at least 96%, at least 97%, at least 98%, at least 99%, or100%. In a further embodiment, the polypeptide has been isolated.

In a continuation of the second aspect, the invention relates tovariants of SEQ ID NO: 12 having arabinofuranosidase activity comprisingone or more amino acid substitutions, and/or one or more amino aciddeletions, and/or one or more amino acid insertions or any combinationthereof at one or more (e.g., several) positions. In an embodiment, thenumber of positions comprising one or more amino acid substitutions,and/or one or more amino acid deletions, and/or one or more amino acidinsertions or any combination thereof in SEQ ID NO: 12 is not more than45, e.g., 1, 2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, 15, 16, 17, 18,19, 20, 21, 22, 23, 24, 25, 26, 27, 28, 29, 30, 31, 32, 33, 34, 35, 36,37, 38, 39, 40, 41, 42, 43, 44 or 45. In an embodiment, the number ofpositions comprising one or more amino acid substitutions, and/or one ormore amino acid deletions, and/or one or more amino acid insertions orany combination thereof in SEQ ID NO: 12 is not more than 10, e.g., 1,2, 3, 4, 5, 6, 7, 8, 9 or 10. In another embodiment, the number ofsubstitutions, deletions, and/or insertions in SEQ ID NO: 12 is not morethan 10, e.g., 1, 2, 3, 4, 5, 6, 7, 8, 9 or 10. In a further embodiment,the number of substitutions, preferably conservative substitutions, inSEQ ID NO: 12 is not more than 10, e.g., 1, 2, 3, 4, 5, 6, 7, 8, 9 or10. In an embodiment, the variant has at least 60%, at least 70%, atleast 75%, at least 80%, at least 85%, at least 90%, at least 95%, or atleast 100% of the activity of the polypeptide of SEQ ID NO: 12.

The amino acid changes may be of a minor nature, that is conservativeamino acid substitutions or insertions that do not significantly affectthe folding and/or activity of the protein; small deletions, typicallyof 1-30 amino acids; small amino- or carboxyl-terminal extensions, suchas an amino-terminal methionine residue; a small linker peptide of up to20-25 residues; or a small extension that facilitates purification bychanging net charge or another function, such as a poly-histidine tract,an antigenic epitope or a binding domain.

Examples of conservative substitutions are within the groups of basicamino acids (arginine, lysine and histidine), acidic amino acids(glutamic acid and aspartic acid), polar amino acids (glutamine andasparagine), hydrophobic amino acids (leucine, isoleucine and valine),aromatic amino acids (phenylalanine, tryptophan and tyrosine), and smallamino acids (glycine, alanine, serine, threonine and methionine). Aminoacid substitutions that do not generally alter specific activity areknown in the art and are described, for example, by H. Neurath and R. L.Hill, 1979, In, The Proteins, Academic Press, New York. Commonsubstitutions are Ala/Ser, Val/Ile, Asp/Glu, Thr/Ser, Ala/Gly, Ala/Thr,Ser/Asn, Ala/Val, Ser/Gly, Tyr/Phe, Ala/Pro, Lys/Arg, Asp/Asn, Leu/Ile,Leu/Val, Ala/Glu, and Asp/Gly.

Alternatively, the amino acid changes are of such a nature that thephysico-chemical properties of the polypeptides are altered. Forexample, amino acid changes may improve the thermal stability of thepolypeptide, alter the substrate specificity, change the pH optimum, andthe like.

Essential amino acids in a polypeptide can be identified according toprocedures known in the art, such as site-directed mutagenesis oralanine-scanning mutagenesis (Cunningham and Wells, 1989, Science 244:1081-1085). In the latter technique, single alanine mutations areintroduced at every residue in the molecule, and the resultant mutantmolecules are tested for arabinofuranosidase activity to identify aminoacid residues that are critical to the activity of the molecule. Seealso, Hilton et al., 1996, J. Biol. Chem. 271: 4699-4708. The activesite of the enzyme or other biological interaction can also bedetermined by physical analysis of structure, as determined by suchtechniques as nuclear magnetic resonance, crystallography, electrondiffraction, or photoaffinity labelling, in conjunction with mutation ofputative contact site amino acids. See, for example, de Vos et al.,1992, Science 255: 306-312; Smith et al., 1992, J. Mol. Biol. 224:899-904; Wlodaver et al., 1992, FEBS Lett. 309: 59-64. The identity ofessential amino acids can also be inferred from an alignment with arelated polypeptide.

Single or multiple amino acid substitutions, deletions, and/orinsertions can be made and tested using known methods of mutagenesis,recombination, and/or shuffling, followed by a relevant screeningprocedure, such as those disclosed by Reidhaar-Olson and Sauer, 1988,Science 241: 53-57; Bowie and Sauer, 1989, Proc. Natl. Acad. Sci. USA86: 2152-2156; WO 95/17413; or WO 95/22625. Other methods that can beused include error-prone PCR, phage display (e.g., Lowman et al., 1991,Biochemistry 30: 10832-10837; U.S. Pat. No. 5,223,409; WO 92/06204), andregion-directed mutagenesis (Derbyshire et al., 1986, Gene 46: 145; Neret al., 1988, DNA 7: 127).

Mutagenesis/shuffling methods can be combined with high-throughput,automated screening methods to detect activity of cloned, mutagenizedpolypeptides expressed by host cells (Ness et al., 1999, NatureBiotechnology 17: 893-896). Mutagenized DNA molecules that encode activepolypeptides can be recovered from the host cells and rapidly sequencedusing standard methods in the art. These methods allow the rapiddetermination of the importance of individual amino acid residues in apolypeptide.

The polypeptide may be a hybrid polypeptide in which a region of onepolypeptide is fused at the N-terminus or the C-terminus of a region ofanother polypeptide.

The polypeptide may be a fusion polypeptide or cleavable fusionpolypeptide in which another polypeptide is fused at the N-terminus orthe C-terminus of the polypeptide of the present invention. A fusionpolypeptide is produced by fusing a polynucleotide encoding anotherpolypeptide to a polynucleotide of the present invention. Techniques forproducing fusion polypeptides are known in the art, and include ligatingthe coding sequences encoding the polypeptides so that they are in frameand that expression of the fusion polypeptide is under control of thesame promoter(s) and terminator. Fusion polypeptides may also beconstructed using intein technology in which fusion polypeptides arecreated post-translationally (Cooper et al., 1993, EMBO J. 12:2575-2583; Dawson et al., 1994, Science 266: 776-779).

A fusion polypeptide can further comprise a cleavage site between thetwo polypeptides. Upon secretion of the fusion protein, the site iscleaved releasing the two polypeptides. Examples of cleavage sitesinclude, but are not limited to, the sites disclosed in Martin et al.,2003, J. Ind. Microbiol. Biotechnol. 3: 568-576; Svetina et al., 2000,J. Biotechnol. 76: 245-251; Rasmussen-Wilson et al., 1997, Appl.Environ. Microbiol. 63: 3488-3493; Ward et al., 1995, Biotechnology 13:498-503; and Contreras et al., 1991, Biotechnology 9: 378-381; Eaton etal., 1986, Biochemistry 25: 505-512; Collins-Racie et al., 1995,Biotechnology 13: 982-987; Carter et al., 1989, Proteins: Structure,Function, and Genetics 6: 240-248; and Stevens, 2003, Drug DiscoveryWorld 4: 35-48.

Carbohydrate molecules are often attached to a polypeptide from a fungalsource during post-translational modification. In order to aid massspectrometry analysis, the polypeptide can be incubated with anendoglycosidase to deglycosylate each N-linked position. For everydeglycosylated N-linked site, one N-acetyl hexosamine remains on theprotein backbone.

In an embodiment, the polypeptide of the second aspect comprises themotif [H/Y][L/M]F[F/S][A/C/H/S/T/V][A/D/G/N/R]D[D/E/N]G (SEQ ID NO: 1),preferably the motif [H/Y]LF[F/S][A/S/V][A/D/G]DNG (SEQ ID NO: 2), morepreferable the motif YLFF[A/V][A/G]DNG (SEQ ID NO: 3), or even morepreferably the motif YLFFAGDNG (SEQ ID NO: 4).

In a third aspect, the invention relates to polypeptides havingarabinofuranosidase activity and having a sequence identity to themature polypeptide of SEQ ID NO: 23 of at least 97.6%, e.g., at least97.9%, at least 98.2%, at least 98.5%, at least 98.8%, at least 91.1%,at least 99.4%, at least 99.7%, which have arabinofuranosidase activity.In one embodiment, the polypeptides differ by up to 7 amino acids, e.g.,between 1 and 7 amino acids, such as 1, 2, 3, 4, 5, 6 or 7 amino acidsfrom the mature polypeptide of SEQ ID NO: 23.

In a continuation of the third aspect, the invention further relates topolypeptides having a sequence identity to SEQ ID NO: 24 of at least97.6% which have arabinofuranosidase activity. In an embodiment, thepolypeptide has a sequence identity to SEQ ID NO: 24 of at least 97.9%.In an embodiment, the polypeptide has a sequence identity to SEQ ID NO:24 of at least 98.2%. In an embodiment, the polypeptide has a sequenceidentity to SEQ ID NO: 24 of at least 98.5%. In an embodiment, thepolypeptide has a sequence identity to SEQ ID NO: 24 of at least 98.8%.In an embodiment, the polypeptide has a sequence identity to SEQ ID NO:24 of at least 99.1%. In an embodiment, the polypeptide has a sequenceidentity to SEQ ID NO: 24 of at least 99.4%. In an embodiment, thepolypeptide has a sequence identity to SEQ ID NO: 24 of at least 99.7%.

In one embodiment, the polypeptides differ by up to 7 amino acids, e.g.,between 1 and 7 amino acids, such as 1, 2, 3, 4, 5, 6 or 7 amino acidsfrom SEQ ID NO: 24. In an embodiment, the polypeptide has at least 60%,at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, atleast 95%, or at least 100% of the activity of the polypeptide of SEQ IDNO: 24.

In one embodiment, the polypeptide preferably comprises or consists ofthe amino acid sequence of SEQ ID NO: 23 and/or SEQ ID NO: 24 or anallelic variant thereof; comprises the amino acid sequence of SEQ ID NO:23 and/or SEQ ID NO: 24 and a N-terminal and/or C-terminal His-tagand/or HQ-tag; or is a fragment thereof having arabinofuranosidaseactivity and having at least 90% such as at least 91%, at least 92%, atleast 93%, at least 94%, at least 95%, at least 96%, at least 97%, atleast 98% or at least 99% of the length of the mature polypeptide. Inanother embodiment, the polypeptide comprises or consists of the maturepolypeptide of SEQ ID NO: 24. In another embodiment, the polypeptidecomprises or consists of amino acids 1 to 302 of SEQ ID NO: 23. Inanother embodiment, the polypeptide comprises or consists of amino acids1 to 302 of SEQ ID NO: 24. In an embodiment, the polypeptide has beenisolated.

In a continuation of the third aspect, the invention relates to apolypeptide having arabinofuranosidase activity encoded by apolynucleotide that hybridizes under very high stringency conditionswith (i) the mature polypeptide coding sequence of SEQ ID NO: 22 or (ii)the full-length complement of (i). In an embodiment, the polypeptide hasbeen isolated.

In a continuation of the third aspect, the invention relates to apolypeptide having arabinofuranosidase activity encoded by apolynucleotide having a sequence identity to the mature polypeptidecoding sequence of SEQ ID NO: 22 or the cDNA sequence thereof of atleast 97.6%, e.g., at least 97.9%, at least 98.2%, at least 98.5%, atleast 98.8%, at least 91.1%, at least 99.4%, at least 99.7%, or 100%. Ina further embodiment, the polypeptide has been isolated.

In a continuation of the third aspect, the invention relates to variantsof SEQ ID NO: 24 having arabinofuranosidase activity comprising one ormore amino acid substitutions, and/or one or more amino acid deletions,and/or one or more amino acid insertions or any combination thereof atone or more (e.g., several) positions. In an embodiment, the number ofpositions comprising one or more amino acid substitutions, and/or one ormore amino acid deletions, and/or one or more amino acid insertions orany combination thereof in SEQ ID NO: 24 is not more than 7, e.g., 1, 2,3, 4, 5, 6 or 7. In another embodiment, the number of substitutions,deletions, and/or insertions in SEQ ID NO: 24 is not more than 7, e.g.,1, 2, 3, 4, 5, 6 or 7. In a further embodiment, the number ofsubstitutions, preferably conservative substitutions, in SEQ ID NO: 24is not more than 7, e.g., 1, 2, 3, 4, 5, 6 or 7. In an embodiment, thevariant has at least 60%, at least 70%, at least 75%, at least 80%, atleast 85%, at least 90%, at least 95%, or at least 100% of the activityof the polypeptide of SEQ ID NO: 24. Examples of amino acid changes andconservative substitutions are described in the second aspect of theinvention.

In an embodiment, the polypeptide of the third aspect comprises themotif [H/Y][L/M]F[F/S][A/C/H/S/T/V][A/D/G/N/R]D[D/E/N]G (SEQ ID NO: 1),preferably the motif [H/Y]LF[F/S][A/S/V][A/D/G]DNG (SEQ ID NO: 2), morepreferable the motif YLFF[A/V][A/G]DNG (SEQ ID NO: 3), or even morepreferably the motif YLFFAGDNG (SEQ ID NO: 4).

In a fourth aspect, the invention relates to polypeptides havingarabinofuranosidase activity and having a sequence identity to themature polypeptide of SEQ ID NO: 26 of at least 80%, e.g., at least 85%,at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, atleast 91%, at least 92%, at least 93%, at least 94%, at least 95%, atleast 96%, at least 97%, at least 98%, at least 99%, which havearabinofuranosidase activity. In one embodiment, the polypeptides differby up to 50 amino acids, e.g., between 1 and 50 amino acids, such as1-45, 1-40, 1-35, 1-30, 1-25, 1-20, 1-15, 1-10 or 1-5 amino acids, or 1,2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, 15, 16, 17, 18, 19, 20, 21,22, 23, 24, 25, 26, 27, 28, 29, 30, 31, 32, 33, 34, 35, 36, 37, 38, 39,40, 41, 42, 43, 44, 45, 46, 47, 48, 49 or 50 amino acids from the maturepolypeptide of SEQ ID NO: 26.

In a continuation of the fourth aspect, the invention further relates topolypeptides having a sequence identity to SEQ ID NO: 27 of at least 80%which have arabinofuranosidase activity. In an embodiment, thepolypeptide has a sequence identity to SEQ ID NO: 27 of at least 85%. Inan embodiment, the polypeptide has a sequence identity to SEQ ID NO: 27of at least 86%. In an embodiment, the polypeptide has a sequenceidentity to SEQ ID NO: 27 of at least 87%. In an embodiment, thepolypeptide has a sequence identity to SEQ ID NO: 27 of at least 88%. Inan embodiment, the polypeptide has a sequence identity to SEQ ID NO: 27of at least 89%. In an embodiment, the polypeptide has a sequenceidentity to SEQ ID NO: 27 of at least 90%. In an embodiment, thepolypeptide has a sequence identity to SEQ ID NO: 27 of at least 91%. Inan embodiment, the polypeptide has a sequence identity to SEQ ID NO: 27of at least 92%. In an embodiment, the polypeptide has a sequenceidentity to SEQ ID NO: 27 of at least 93%. In an embodiment, thepolypeptide has a sequence identity to SEQ ID NO: 27 of at least 94%. Inan embodiment, the polypeptide has a sequence identity to SEQ ID NO: 27of at least 95%. In an embodiment, the polypeptide has a sequenceidentity to SEQ ID NO: 27 of at least 96%. In an embodiment, thepolypeptide has a sequence identity to SEQ ID NO: 27 of at least 97%. Inan embodiment, the polypeptide has a sequence identity to SEQ ID NO: 27of at least 98%. In an embodiment, the polypeptide has a sequenceidentity to SEQ ID NO: 27 of at least 99%.

In one embodiment, the polypeptides differ by up to 50 amino acids,e.g., between 1 and 50 amino acids, such as 1-45, 1-40, 1-35, 1-30,1-25, 1-20, 1-15, 1-10 or 1-5 amino acids, or 1, 2, 3, 4, 5, 6, 7, 8, 9,10, 11, 12, 13, 14, 15, 16, 17, 18, 19, 20, 21, 22, 23, 24, 25, 26, 27,28, 29, 30, 31, 32, 33, 34, 35, 36, 37, 38, 39, 40, 41, 42, 43, 44, 45,46, 47, 48, 49 or 50 amino acids from SEQ ID NO: 27. In an embodiment,the polypeptide has at least 60%, at least 70%, at least 75%, at least80%, at least 85%, at least 90%, at least 95%, or at least 100% of theactivity of the polypeptide of SEQ ID NO: 27.

In one embodiment, the polypeptide preferably comprises or consists ofthe amino acid sequence of SEQ ID NO: 26 and/or SEQ ID NO: 27 or anallelic variant thereof; comprises the amino acid sequence of SEQ ID NO:26 and/or SEQ ID NO: 27 and a N-terminal and/or C-terminal His-tagand/or HQ-tag; or is a fragment thereof having arabinofuranosidaseactivity and having at least 90% such as at least 91%, at least 92%, atleast 93%, at least 94%, at least 95%, at least 96%, at least 97%, atleast 98% or at least 99% of the length of the mature polypeptide. Inanother embodiment, the polypeptide comprises or consists of the maturepolypeptide of SEQ ID NO: 27. In another embodiment, the polypeptidecomprises or consists of amino acids 1 to 309 of SEQ ID NO: 26. Inanother embodiment, the polypeptide comprises or consists of amino acids1 to 309 of SEQ ID NO: 27. In an embodiment, the polypeptide has beenisolated.

In a continuation of the fourth aspect, the invention relates to apolypeptide having arabinofuranosidase activity encoded by apolynucleotide that hybridizes under high stringency conditions or veryhigh stringency conditions with (i) the mature polypeptide codingsequence of SEQ ID NO: 25 or (ii) the full-length complement of (i). Inan embodiment, the polypeptide has been isolated.

In a continuation of the fourth aspect, the invention relates to apolypeptide having arabinofuranosidase activity encoded by apolynucleotide having a sequence identity to the mature polypeptidecoding sequence of SEQ ID NO: 25 or the cDNA sequence thereof of atleast 80%, e.g., at least 85%, at least 86%, at least 87%, at least 88%,at least 89%, at least 90%, at least 91%, at least 92%, at least 93%, atleast 94%, at least 95%, at least 96%, at least 97%, at least 98%, atleast 99%, or 100%. In a further embodiment, the polypeptide has beenisolated.

In a continuation of the fourth aspect, the invention relates tovariants of SEQ ID NO: 27 having arabinofuranosidase activity comprisingone or more amino acid substitutions, and/or one or more amino aciddeletions, and/or one or more amino acid insertions or any combinationthereof at one or more (e.g., several) positions. In an embodiment, thenumber of positions comprising one or more amino acid substitutions,and/or one or more amino acid deletions, and/or one or more amino acidinsertions or any combination thereof in SEQ ID NO: 27 is not more than50, e.g., 1, 2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, 15, 16, 17, 18,19, 20, 21, 22, 23, 24, 25, 26, 27, 28, 29, 30, 31, 32, 33, 34, 35, 36,37, 38, 39, 40, 41, 42, 43, 44, 45, 46, 47, 48, 49 or 50. In anembodiment, the number of positions comprising one or more amino acidsubstitutions, and/or one or more amino acid deletions, and/or one ormore amino acid insertions or any combination thereof in SEQ ID NO: 27is not more than 10, e.g., 1, 2, 3, 4, 5, 6, 7, 8, 9 or 10. In anotherembodiment, the number of substitutions, deletions, and/or insertions inSEQ ID NO: 27 is not more than 10, e.g., 1, 2, 3, 4, 5, 6, 7, 8, 9 or10. In a further embodiment, the number of substitutions, preferablyconservative substitutions, in SEQ ID NO: 27 is not more than 10, e.g.,1, 2, 3, 4, 5, 6, 7, 8, 9 or 10. In an embodiment, the variant has atleast 60%, at least 70%, at least 75%, at least 80%, at least 85%, atleast 90%, at least 95%, or at least 100% of the activity of thepolypeptide of SEQ ID NO: 27. Examples of amino acid changes andconservative substitutions are described in the second aspect of theinvention.

In an embodiment, the polypeptide of the fourth aspect comprises themotif [H/Y][L/M]F[F/S][A/C/H/S/T/V][A/D/G/N/R]D[D/E/N]G (SEQ ID NO: 1),preferably the motif [H/Y]LF[F/S][A/S/V][A/D/G]DNG (SEQ ID NO: 2), morepreferable the motif YLFF[A/V][A/G]DNG (SEQ ID NO: 3), or even morepreferably the motif YLFFAGDNG (SEQ ID NO: 4).

In a fifth aspect, the invention relates to polypeptides havingarabinofuranosidase activity and having a sequence identity to themature polypeptide of SEQ ID NO: 29 of at least 90%, e.g., at least 91%,at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, atleast 97%, at least 98%, at least 99%, which have arabinofuranosidaseactivity. In one embodiment, the polypeptides differ by up to 43 aminoacids, e.g., between 1 and 43 amino acids, such as 1-40, 1-35, 1-30,1-25, 1-20, 1-15, 1-10 or 1-5 amino acids, or 1, 2, 3, 4, 5, 6, 7, 8, 9,10, 11, 12, 13, 14, 15, 16, 17, 18, 19, 20, 21, 22, 23, 24, 25, 26, 27,28, 29, 30, 31, 32, 33, 34, 35, 36, 37, 38, 39, 40, 41, 42 or 43 aminoacids from the mature polypeptide of SEQ ID NO: 29.

In a continuation of the fifth aspect, the invention further relates topolypeptides having a sequence identity to SEQ ID NO: 30 of at least 90%which have arabinofuranosidase activity. In an embodiment, thepolypeptide has a sequence identity to SEQ ID NO: 30 of at least 91%. Inan embodiment, the polypeptide has a sequence identity to SEQ ID NO: 30of at least 92%. In an embodiment, the polypeptide has a sequenceidentity to SEQ ID NO: 30 of at least 93%. In an embodiment, thepolypeptide has a sequence identity to SEQ ID NO: 30 of at least 94%. Inan embodiment, the polypeptide has a sequence identity to SEQ ID NO: 30of at least 95%. In an embodiment, the polypeptide has a sequenceidentity to SEQ ID NO: 30 of at least 96%. In an embodiment, thepolypeptide has a sequence identity to SEQ ID NO: 30 of at least 97%. Inan embodiment, the polypeptide has a sequence identity to SEQ ID NO: 30of at least 98%. In an embodiment, the polypeptide has a sequenceidentity to SEQ ID NO: 30 of at least 99%.

In one embodiment, the polypeptides differ by up to 43 amino acids, suchas 1-40, 1-35, 1-30, 1-25, 1-20, 1-15, 1-10 or 1-5 amino acids, or 1, 2,3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, 15, 16, 17, 18, 19, 20, 21, 22,23, 24, 25, 26, 27, 28, 29, 30, 31, 32, 33, 34, 35, 36, 37, 38, 39, 40,41, 42 or 43 amino acids from SEQ ID NO: 30. In one embodiment, thepolypeptides differ by up to 43 amino acids, such as 1-40, 1-35, 1-30,1-25, 1-20, 1-15, 1-10 or 1-5 amino acids, or 1, 2, 3, 4, 5, 6, 7, 8, 9,10, 11, 12, 13, 14, 15, 16, 17, 18, 19, 20, 21, 22, 23, 24, 25, 26, 27,28, 29, 30, 31, 32, 33, 34, 35, 36, 37, 38, 39, 40, 41, 42 or 43 aminoacids from SEQ ID NO: 33. In an embodiment, the polypeptide has at least60%, at least 70%, at least 75%, at least 80%, at least 85%, at least90%, at least 95%, or at least 100% of the activity of the polypeptideof SEQ ID NO: 30.

In one embodiment, the polypeptide preferably comprises or consists ofthe amino acid sequence of SEQ ID NO: 29 and/or SEQ ID NO: 30 or anallelic variant thereof; comprises the amino acid sequence of SEQ ID NO:29 and/or SEQ ID NO: 30 and a N-terminal and/or C-terminal His-tagand/or HQ-tag such as SEQ ID NO: 33; or is a fragment thereof havingarabinofuranosidase activity and having at least 90% such as at least91%, at least 92%, at least 93%, at least 94%, at least 95%, at least96%, at least 97%, at least 98% or at least 99% of the length of themature polypeptide. In another embodiment, the polypeptide comprises orconsists of the mature polypeptide of SEQ ID NO: 29. In anotherembodiment, the polypeptide comprises or consists of the maturepolypeptide of SEQ ID NO: 32. In another embodiment, the polypeptidecomprises or consists of amino acids 1 to 438 of SEQ ID NO: 29. Inanother embodiment, the polypeptide comprises or consists of amino acids1 to 438 of SEQ ID NO: 30. In another embodiment, the polypeptidecomprises or consists of amino acids 1 to 446 of SEQ ID NO: 32. Inanother embodiment, the polypeptide comprises or consists of amino acids1 to 446 of SEQ ID NO: 33. In an embodiment, the polypeptide has beenisolated.

In a continuation of the fifth aspect, the invention relates to apolypeptide having arabinofuranosidase activity encoded by apolynucleotide that hybridizes under high stringency conditions or veryhigh stringency conditions with (i) the mature polypeptide codingsequence of SEQ ID NO: 28 or (ii) the full-length complement of (i). Inan embodiment, the polypeptide has been isolated.

In a continuation of the fifth aspect, the invention relates to apolypeptide having arabinofuranosidase activity encoded by apolynucleotide having a sequence identity to the mature polypeptidecoding sequence of SEQ ID NO: 28 or the cDNA sequence thereof of atleast 90%, e.g., at least 91%, at least 92%, at least 93%, at least 94%,at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or100%. In a further embodiment, the polypeptide has been isolated.

In a continuation of the fifth aspect, the invention relates to variantsof SEQ ID NO: 30 having arabinofuranosidase activity comprising one ormore amino acid substitutions, and/or one or more amino acid deletions,and/or one or more amino acid insertions or any combination thereof atone or more (e.g., several) positions. In an embodiment, the number ofpositions comprising one or more amino acid substitutions, and/or one ormore amino acid deletions, and/or one or more amino acid insertions orany combination thereof in SEQ ID NO: 30 is not more than 45, e.g., 1,2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, 15, 16, 17, 18, 19, 20, 21,22, 23, 24, 25, 26, 27, 28, 29, 30, 31, 32, 33, 34, 35, 36, 37, 38, 39,40, 41, 42, 43, 44 or 45. In an embodiment, the number of positionscomprising one or more amino acid substitutions, and/or one or moreamino acid deletions, and/or one or more amino acid insertions or anycombination thereof in SEQ ID NO: 30 is not more than 10, e.g., 1, 2, 3,4, 5, 6, 7, 8, 9 or 10. In another embodiment, the number ofsubstitutions, deletions, and/or insertions in SEQ ID NO: 30 is not morethan 10, e.g., 1, 2, 3, 4, 5, 6, 7, 8, 9 or 10. In a further embodiment,the number of substitutions, preferably conservative substitutions, inSEQ ID NO: 30 is not more than 10, e.g., 1, 2, 3, 4, 5, 6, 7, 8, 9 or10. In an embodiment, the variant has at least 60%, at least 70%, atleast 75%, at least 80%, at least 85%, at least 90%, at least 95%, or atleast 100% of the activity of the polypeptide of SEQ ID NO: 30. Examplesof amino acid changes and conservative substitutions are described inthe second aspect of the invention.

In an embodiment, the polypeptide of the fifth aspect comprises themotif [H/Y][L/M]F[F/S][A/C/H/S/T/V][A/D/G/N/R]D[D/E/N]G (SEQ ID NO: 1),preferably the motif [H/Y]LF[F/S][A/S/V][A/D/G]DNG (SEQ ID NO: 2), morepreferable the motif YLFF[A/V][A/G]DNG (SEQ ID NO: 3), or even morepreferably the motif YLFFAGDNG (SEQ ID NO: 4).

In a sixth aspect, the invention relates to polypeptides havingarabinofuranosidase activity and having a sequence identity to themature polypeptide of SEQ ID NO: 35 of at least 92%, e.g. at least 93%,at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, atleast 99%, which have arabinofuranosidase activity. In one embodiment,the polypeptides differ by up to 34 amino acids, e.g., between 1 and 34amino acids, such as 1-30, 1-25, 1-20, 1-15, 1-10 or 1-5 amino acids, or1, 2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, 15, 16, 17, 18, 19, 20,21, 22, 23, 24, 25, 26, 27, 28, 29, 30, 31, 32, 33 or 34 amino acidsfrom the mature polypeptide of SEQ ID NO: 35.

In one embodiment, the polypeptides differ by up to 34 amino acids,e.g., between 1 and 34 amino acids, such as 1-30, 1-25, 1-20, 1-15, 1-10or 1-5 amino acids, or 1, 2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13, 14,15, 16, 17, 18, 19, 20, 21, 22, 23, 24, 25, 26, 27, 28, 29, 30, 31, 32,33 or 34 amino acids from SEQ ID NO: 36. In one embodiment, thepolypeptides differ by up to 34 amino acids, e.g., between 1 and 34amino acids, such as 1-30, 1-25, 1-20, 1-15, 1-10 or 1-5 amino acids, or1, 2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, 15, 16, 17, 18, 19, 20,21, 22, 23, 24, 25, 26, 27, 28, 29, 30, 31, 32, 33 or 34 amino acidsfrom SEQ ID NO: 39. In an embodiment, the polypeptide has at least 60%,at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, atleast 95%, or at least 100% of the activity of the polypeptide of SEQ IDNO: 36.

In one embodiment, the polypeptide preferably comprises or consists ofthe amino acid sequence of SEQ ID NO: 35 and/or SEQ ID NO: 36 or anallelic variant thereof; comprises the amino acid sequence of SEQ ID NO:35 and/or SEQ ID NO: 36 and a N-terminal and/or C-terminal His-tagand/or HQ-tag such as SEQ ID NO: 39; or is a fragment thereof havingarabinofuranosidase activity and having at least 90% such as at least91%, at least 92%, at least 93%, at least 94%, at least 95%, at least96%, at least 97%, at least 98% or at least 99% of the length of themature polypeptide. In another embodiment, the polypeptide comprises orconsists of the mature polypeptide of SEQ ID NO: 35. In anotherembodiment, the polypeptide comprises or consists of the maturepolypeptide of SEQ ID NO: 38. In another embodiment, the polypeptidecomprises or consists of amino acids 1 to 438 of SEQ ID NO: 35. Inanother embodiment, the polypeptide comprises or consists of amino acids1 to 438 of SEQ ID NO: 36. In another embodiment, the polypeptidecomprises or consists of amino acids 1 to 446 of SEQ ID NO: 38. Inanother embodiment, the polypeptide comprises or consists of amino acids1 to 446 of SEQ ID NO: 39. In an embodiment, the polypeptide has beenisolated.

In a continuation of the sixth aspect, the invention relates to apolypeptide having arabinofuranosidase activity encoded by apolynucleotide that hybridizes under high stringency conditions or veryhigh stringency conditions with (i) the mature polypeptide codingsequence of SEQ ID NO: 34 or (ii) the full-length complement of (i). Inan embodiment, the polypeptide has been isolated.

In a continuation of the sixth aspect, the invention relates to apolypeptide having arabinofuranosidase activity encoded by apolynucleotide having a sequence identity to the mature polypeptidecoding sequence of SEQ ID NO: 34 or the cDNA sequence thereof of atleast 92%, e.g., at least 93%, at least 94%, at least 95%, at least 96%,at least 97%, at least 98%, at least 99%, or 100%. In a furtherembodiment, the polypeptide has been isolated.

In a continuation of the sixth aspect, the invention relates to variantsof SEQ ID NO: 36 having arabinofuranosidase activity comprising one ormore amino acid substitutions, and/or one or more amino acid deletions,and/or one or more amino acid insertions or any combination thereof atone or more (e.g., several) positions. In an embodiment, the number ofpositions comprising one or more amino acid substitutions, and/or one ormore amino acid deletions, and/or one or more amino acid insertions orany combination thereof in SEQ ID NO: 36 is not more than 34, e.g., 1,2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, 15, 16, 17, 18, 19, 20, 21,22, 23, 24, 25, 26, 27, 28, 29, 30, 31, 32, 33 or 34. In an embodiment,the number of positions comprising one or more amino acid substitutions,and/or one or more amino acid deletions, and/or one or more amino acidinsertions or any combination thereof in SEQ ID NO: 36 is not more than10, e.g., 1, 2, 3, 4, 5, 6, 7, 8, 9 or 10. In another embodiment, thenumber of substitutions, deletions, and/or insertions in SEQ ID NO: 36is not more than 10, e.g., 1, 2, 3, 4, 5, 6, 7, 8, 9 or 10. In a furtherembodiment, the number of substitutions, preferably conservativesubstitutions, in SEQ ID NO: 36 is not more than 10, e.g., 1, 2, 3, 4,5, 6, 7, 8, 9 or 10. In an embodiment, the variant has at least 60%, atleast 70%, at least 75%, at least 80%, at least 85%, at least 90%, atleast 95%, or at least 100% of the activity of the polypeptide of SEQ IDNO: 36. Examples of amino acid changes and conservative substitutionsare described in the second aspect of the invention.

In an embodiment, the polypeptide of the sixth aspect comprises themotif [H/Y][L/M]F[F/S][A/C/H/S/T/V][A/D/G/N/R]D[D/E/N]G (SEQ ID NO: 1),preferably the motif [H/Y]LF[F/S][A/S/V][A/D/G]DNG (SEQ ID NO: 2), morepreferable the motif YLFF[A/V][A/G]DNG (SEQ ID NO: 3), or even morepreferably the motif YLFFAGDNG (SEQ ID NO: 4).

In a seventh aspect, the invention relates to polypeptides havingarabinofuranosidase activity and having a sequence identity to themature polypeptide of SEQ ID NO: 47 of at least 86%, e.g., at least 87%,at least 88%, at least 89%, at least 90%, at least 91%, at least 92%, atleast 93%, at least 94%, at least 95%, at least 96%, at least 97%, atleast 98%, at least 99%, which have arabinofuranosidase activity. In oneembodiment, the polypeptides differ by up to 42 amino acids, e.g.,between 1 and 42 amino acids, such as 1-35, 1-30, 1-25, 1-20, 1-15, 1-10or 1-5 amino acids, or 1, 2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13, 14,15, 16, 17, 18, 19, 20, 21, 22, 23, 24, 25, 26, 27, 28, 29, 30, 31, 32,33, 34, 35, 36, 37, 38, 39, 40, 41 or 42 amino acids from the maturepolypeptide of SEQ ID NO: 47.

In a continuation of the seventh aspect, the invention further relatesto polypeptides having a sequence identity to SEQ ID NO: 48 of at least86% which have arabinofuranosidase activity. In an embodiment, thepolypeptide has a sequence identity to SEQ ID NO: 48 of at least 87%. Inan embodiment, the polypeptide has a sequence identity to SEQ ID NO: 48of at least 88%. In an embodiment, the polypeptide has a sequenceidentity to SEQ ID NO: 48 of at least 89%. In an embodiment, thepolypeptide has a sequence identity to SEQ ID NO: 48 of at least 90%. Inan embodiment, the polypeptide has a sequence identity to SEQ ID NO: 48of at least 91%. In an embodiment, the polypeptide has a sequenceidentity to SEQ ID NO: 48 of at least 92%. In an embodiment, thepolypeptide has a sequence identity to SEQ ID NO: 48 of at least 93%. Inan embodiment, the polypeptide has a sequence identity to SEQ ID NO: 48of at least 94%. In an embodiment, the polypeptide has a sequenceidentity to SEQ ID NO: 48 of at least 95%. In an embodiment, thepolypeptide has a sequence identity to SEQ ID NO: 48 of at least 96%. Inan embodiment, the polypeptide has a sequence identity to SEQ ID NO: 48of at least 97%. In an embodiment, the polypeptide has a sequenceidentity to SEQ ID NO: 48 of at least 98%. In an embodiment, thepolypeptide has a sequence identity to SEQ ID NO: 48 of at least 99%.

In one embodiment, the polypeptides differ by up to 42 amino acids,e.g., between 1 and 42 amino acids, such as 1-35, 1-30, 1-25, 1-20,1-15, 1-10 or 1-5 amino acids, or 1, 2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12,13, 14, 15, 16, 17, 18, 19, 20, 21, 22, 23, 24, 25, 26, 27, 28, 29, 30,31, 32, 33, 34, 35, 36, 37, 38, 39, 40, 41 or 42 amino acids from SEQ IDNO: 48. In one embodiment, the polypeptides differ by up to 42 aminoacids, e.g., between 1 and 42 amino acids, such as 1-35, 1-30, 1-25,1-20, 1-15, 1-10 or 1-5 amino acids, or 1, 2, 3, 4, 5, 6, 7, 8, 9, 10,11, 12, 13, 14, 15, 16, 17, 18, 19, 20, 21, 22, 23, 24, 25, 26, 27, 28,29, 30, 31, 32, 33, 34, 35, 36, 37, 38, 39, 40, 41 or 42 amino acidsfrom SEQ ID NO: 51. In an embodiment, the polypeptide has at least 60%,at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, atleast 95%, or at least 100% of the activity of the polypeptide of SEQ IDNO: 48.

In one embodiment, the polypeptide preferably comprises or consists ofthe amino acid sequence of SEQ ID NO: 47 and/or SEQ ID NO: 48 or anallelic variant thereof; comprises the amino acid sequence of SEQ ID NO:47 and/or SEQ ID NO: 48 and a N-terminal and/or C-terminal His-tagand/or HQ-tag such as SEQ ID NO: 51; or is a fragment thereof havingarabinofuranosidase activity and having at least 90% such as at least91%, at least 92%, at least 93%, at least 94%, at least 95%, at least96%, at least 97%, at least 98% or at least 99% of the length of themature polypeptide. In another embodiment, the polypeptide comprises orconsists of the mature polypeptide of SEQ ID NO: 47. In anotherembodiment, the polypeptide comprises or consists of the maturepolypeptide of SEQ ID NO: 50. In another embodiment, the polypeptidecomprises or consists of amino acids 1 to 537 of SEQ ID NO: 47. Inanother embodiment, the polypeptide comprises or consists of amino acids1 to 537 of SEQ ID NO: 48. In another embodiment, the polypeptidecomprises or consists of amino acids 1 to 311 of SEQ ID NO: 50. Inanother embodiment, the polypeptide comprises or consists of amino acids1 to 311 of SEQ ID NO: 51. In an embodiment, the polypeptide has beenisolated.

In a continuation of the seventh aspect, the invention relates to apolypeptide having arabinofuranosidase activity encoded by apolynucleotide that hybridizes under high stringency conditions or veryhigh stringency conditions with (i) the mature polypeptide codingsequence of SEQ ID NO: 46 or (ii) the full-length complement of (i). Inan embodiment, the polypeptide has been isolated.

In a continuation of the seventh aspect, the invention relates to apolypeptide having arabinofuranosidase activity encoded by apolynucleotide having a sequence identity to the mature polypeptidecoding sequence of SEQ ID NO: 46 or the cDNA sequence thereof of atleast 86%, e.g. at least 87%, at least 88%, at least 89%, at least 90%,at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, atleast 96%, at least 97%, at least 98%, at least 99%, or 100%. In afurther embodiment, the polypeptide has been isolated.

In a continuation of the seventh aspect, the invention relates tovariants of SEQ ID NO: 48 having arabinofuranosidase activity comprisingone or more amino acid substitutions, and/or one or more amino aciddeletions, and/or one or more amino acid insertions or any combinationthereof at one or more (e.g., several) positions. In an embodiment, thenumber of positions comprising one or more amino acid substitutions,and/or one or more amino acid deletions, and/or one or more amino acidinsertions or any combination thereof in SEQ ID NO: 48 is not more than42, e.g., 1, 2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, 15, 16, 17, 18,19, 20, 21, 22, 23, 24, 25, 26, 27, 28, 29, 30, 31, 32, 33, 34, 35, 36,37, 38, 39, 40, 41 or 42. In an embodiment, the number of positionscomprising one or more amino acid substitutions, and/or one or moreamino acid deletions, and/or one or more amino acid insertions or anycombination thereof in SEQ ID NO: 48 is not more than 10, e.g., 1, 2, 3,4, 5, 6, 7, 8, 9 or 10. In another embodiment, the number ofsubstitutions, deletions, and/or insertions in SEQ ID NO: 48 is not morethan 10, e.g., 1, 2, 3, 4, 5, 6, 7, 8, 9 or 10. In a further embodiment,the number of substitutions, preferably conservative substitutions, inSEQ ID NO: 48 is not more than 10, e.g., 1, 2, 3, 4, 5, 6, 7, 8, 9 or10. In an embodiment, the variant has at least 60%, at least 70%, atleast 75%, at least 80%, at least 85%, at least 90%, at least 95%, or atleast 100% of the activity of the polypeptide of SEQ ID NO: 48. Examplesof amino acid changes and conservative substitutions are described inthe second aspect of the invention.

In an embodiment, the polypeptide of the seventh aspect comprises themotif [H/Y][L/M]F[F/S][A/C/H/S/T/V][A/D/G/N/R]D[D/E/N]G (SEQ ID NO: 1),preferably the motif [H/Y]LF[F/S][A/S/V][A/D/G]DNG (SEQ ID NO: 2), morepreferable the motif YLFF[A/V][A/G]DNG (SEQ ID NO: 3), or even morepreferably the motif YLFFAGDNG (SEQ ID NO: 4).

In an eighth aspect, the invention relates to polypeptides havingarabinofuranosidase activity and having a sequence identity to themature polypeptide of SEQ ID NO: 53 of at least 80%, e.g., at least 85%,at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, atleast 91%, at least 92%, at least 93%, at least 94%, at least 95%, atleast 96%, at least 97%, at least 98%, at least 99%, which havearabinofuranosidase activity. In one embodiment, the polypeptides differby up to 50 amino acids, e.g., between 1 and 50 amino acids, such as1-45, 1-40, 1-35, 1-30, 1-25, 1-20, 1-15, 1-10 or 1-5 amino acids, or 1,2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, 15, 16, 17, 18, 19, 20, 21,22, 23, 24, 25, 26, 27, 28, 29, 30, 31, 32, 33, 34, 35, 36, 37, 38, 39,40, 41, 42, 43, 44, 45, 46, 47, 48, 49 or 50 amino acids from the maturepolypeptide of SEQ ID NO: 53.

In a continuation of the eighth aspect, the invention further relates topolypeptides having a sequence identity to SEQ ID NO: 54 of at least 80%which have arabinofuranosidase activity. In an embodiment, thepolypeptide has a sequence identity to SEQ ID NO: 54 of at least 85%. Inan embodiment, the polypeptide has a sequence identity to SEQ ID NO: 54of at least 86%. In an embodiment, the polypeptide has a sequenceidentity to SEQ ID NO: 54 of at least 87%. In an embodiment, thepolypeptide has a sequence identity to SEQ ID NO: 54 of at least 88%. Inan embodiment, the polypeptide has a sequence identity to SEQ ID NO: 54of at least 89%. In an embodiment, the polypeptide has a sequenceidentity to SEQ ID NO: 54 of at least 90%. In an embodiment, thepolypeptide has a sequence identity to SEQ ID NO: 54 of at least 91%. Inan embodiment, the polypeptide has a sequence identity to SEQ ID NO: 54of at least 92%. In an embodiment, the polypeptide has a sequenceidentity to SEQ ID NO: 54 of at least 93%. In an embodiment, thepolypeptide has a sequence identity to SEQ ID NO: 54 of at least 94%. Inan embodiment, the polypeptide has a sequence identity to SEQ ID NO: 54of at least 95%. In an embodiment, the polypeptide has a sequenceidentity to SEQ ID NO: 54 of at least 96%. In an embodiment, thepolypeptide has a sequence identity to SEQ ID NO: 54 of at least 97%. Inan embodiment, the polypeptide has a sequence identity to SEQ ID NO: 54of at least 98%. In an embodiment, the polypeptide has a sequenceidentity to SEQ ID NO: 54 of at least 99%.

In one embodiment, the polypeptides differ by up to 50 amino acids,e.g., between 1 and 50 amino acids, such as 1-45, 1-40, 1-35, 1-30,1-25, 1-20, 1-15, 1-10 or 1-5 amino acids, or 1, 2, 3, 4, 5, 6, 7, 8, 9,10, 11, 12, 13, 14, 15, 16, 17, 18, 19, 20, 21, 22, 23, 24, 25, 26, 27,28, 29, 30, 31, 32, 33, 34, 35, 36, 37, 38, 39, 40, 41, 42, 43, 44, 45,46, 47, 48, 49 or 50 amino acids from SEQ ID NO: 54. In one embodiment,the polypeptides differ by up to 50 amino acids, e.g., between 1 and 50amino acids, such as 1-45, 1-40, 1-35, 1-30, 1-25, 1-20, 1-15, 1-10 or1-5 amino acids, or 1, 2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, 15,16, 17, 18, 19, 20, 21, 22, 23, 24, 25, 26, 27, 28, 29, 30, 31, 32, 33,34, 35, 36, 37, 38, 39, 40, 41, 42, 43, 44, 45, 46, 47, 48, 49 or 50amino acids from SEQ ID NO: 57. In an embodiment, the polypeptide has atleast 60%, at least 70%, at least 75%, at least 80%, at least 85%, atleast 90%, at least 95%, or at least 100% of the activity of thepolypeptide of SEQ ID NO: 54.

In one embodiment, the polypeptide preferably comprises or consists ofthe amino acid sequence of SEQ ID NO: 53 and/or SEQ ID NO: 54 or anallelic variant thereof; comprises the amino acid sequence of SEQ ID NO:53 and/or SEQ ID NO: 54 and a N-terminal and/or C-terminal His-tagand/or HQ-tag such as SEQ ID NO: 57; or is a fragment thereof havingarabinofuranosidase activity and having at least 90% such as at least91%, at least 92%, at least 93%, at least 94%, at least 95%, at least96%, at least 97%, at least 98% or at least 99% of the length of themature polypeptide. In another embodiment, the polypeptide comprises orconsists of the mature polypeptide of SEQ ID NO: 53. In anotherembodiment, the polypeptide comprises or consists of the maturepolypeptide of SEQ ID NO: 56. In another embodiment, the polypeptidecomprises or consists of amino acids 1 to 364 of SEQ ID NO: 53. Inanother embodiment, the polypeptide comprises or consists of amino acids1 to 364 of SEQ ID NO: 54. In another embodiment, the polypeptidecomprises or consists of amino acids 1 to 373 of SEQ ID NO: 56. Inanother embodiment, the polypeptide comprises or consists of amino acids1 to 373 of SEQ ID NO: 57. In an embodiment, the polypeptide has beenisolated.

In a continuation of the eighth aspect, the invention relates to apolypeptide having arabinofuranosidase activity encoded by apolynucleotide that hybridizes under high stringency conditions or veryhigh stringency conditions with (i) the mature polypeptide codingsequence of SEQ ID NO: 52 or (ii) the full-length complement of (i). Inan embodiment, the polypeptide has been isolated.

In a continuation of the eighth aspect, the invention relates to apolypeptide having arabinofuranosidase activity encoded by apolynucleotide having a sequence identity to the mature polypeptidecoding sequence of SEQ ID NO: 52 or the cDNA sequence thereof of atleast 80%, e.g., at least 85%, at least 86%, at least 87%, at least 88%,at least 89%, at least 90%, at least 91%, at least 92%, at least 93%, atleast 94%, at least 95%, at least 96%, at least 97%, at least 98%, atleast 99%, or 100%. In a further embodiment, the polypeptide has beenisolated.

In a continuation of the eighth aspect, the invention relates tovariants of SEQ ID NO: 54 having arabinofuranosidase activity comprisingone or more amino acid substitutions, and/or one or more amino aciddeletions, and/or one or more amino acid insertions or any combinationthereof at one or more (e.g., several) positions. In an embodiment, thenumber of positions comprising one or more amino acid substitutions,and/or one or more amino acid deletions, and/or one or more amino acidinsertions or any combination thereof in SEQ ID NO: 54 is not more than50, e.g., 1, 2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, 15, 16, 17, 18,19, 20, 21, 22, 23, 24, 25, 26, 27, 28, 29, 30, 31, 32, 33, 34, 35, 36,37, 38, 39, 40, 41, 42, 43, 44, 45, 46, 47, 48, 49 or 50. In anembodiment, the number of positions comprising one or more amino acidsubstitutions, and/or one or more amino acid deletions, and/or one ormore amino acid insertions or any combination thereof in SEQ ID NO: 54is not more than 10, e.g., 1, 2, 3, 4, 5, 6, 7, 8, 9 or 10. In anotherembodiment, the number of substitutions, deletions, and/or insertions inSEQ ID NO: 54 is not more than 10, e.g., 1, 2, 3, 4, 5, 6, 7, 8, 9 or10. In a further embodiment, the number of substitutions, preferablyconservative substitutions, in SEQ ID NO: 54 is not more than 10, e.g.,1, 2, 3, 4, 5, 6, 7, 8, 9 or 10. In an embodiment, the variant has atleast 60%, at least 70%, at least 75%, at least 80%, at least 85%, atleast 90%, at least 95%, or at least 100% of the activity of thepolypeptide of SEQ ID NO: 54. Examples of amino acid changes andconservative substitutions are described in the second aspect of theinvention.

In an embodiment, the polypeptide of the eighth aspect comprises themotif [H/Y][L/M]F[F/S][A/C/H/S/T/V][A/D/G/N/R]D[D/E/N]G (SEQ ID NO: 1),preferably the motif [H/Y]LF[F/S][A/S/V][A/D/G]DNG (SEQ ID NO: 2), morepreferable the motif YLFF[A/V][A/G]DNG (SEQ ID NO: 3), or even morepreferably the motif YLFFAGDNG (SEQ ID NO: 4).

In an ninth aspect, the invention relates to polypeptides havingarabinofuranosidase activity and having a sequence identity to themature polypeptide of SEQ ID NO: 59 of at least 81%, e.g., at least 85%,at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, atleast 91%, at least 92%, at least 93%, at least 94%, at least 95%, atleast 96%, at least 97%, at least 98%, at least 99%, which havearabinofuranosidase activity. In one embodiment, the polypeptides differby up to 50 amino acids, e.g., between 1 and 50 amino acids, such as1-45, 1-40, 1-35, 1-30, 1-25, 1-20, 1-15, 1-10 or 1-5 amino acids, or 1,2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, 15, 16, 17, 18, 19, 20, 21,22, 23, 24, 25, 26, 27, 28, 29, 30, 31, 32, 33, 34, 35, 36, 37, 38, 39,40, 41, 42, 43, 44, 45, 46, 47, 48, 49 or 50 amino acids from the maturepolypeptide of SEQ ID NO: 59.

In a continuation of the ninth aspect, the invention further relates topolypeptides having a sequence identity to SEQ ID NO: 60 of at least 81%which have arabinofuranosidase activity. In an embodiment, thepolypeptide has a sequence identity to SEQ ID NO: 60 of at least 86%. Inan embodiment, the polypeptide has a sequence identity to SEQ ID NO: 60of at least 87%. In an embodiment, the polypeptide has a sequenceidentity to SEQ ID NO: 60 of at least 88%. In an embodiment, thepolypeptide has a sequence identity to SEQ ID NO: 60 of at least 89%. Inan embodiment, the polypeptide has a sequence identity to SEQ ID NO: 60of at least 90%. In an embodiment, the polypeptide has a sequenceidentity to SEQ ID NO: 60 of at least 91%. In an embodiment, thepolypeptide has a sequence identity to SEQ ID NO: 60 of at least 92%. Inan embodiment, the polypeptide has a sequence identity to SEQ ID NO: 60of at least 93%. In an embodiment, the polypeptide has a sequenceidentity to SEQ ID NO: 60 of at least 94%. In an embodiment, thepolypeptide has a sequence identity to SEQ ID NO: 60 of at least 95%. Inan embodiment, the polypeptide has a sequence identity to SEQ ID NO: 60of at least 96%. In an embodiment, the polypeptide has a sequenceidentity to SEQ ID NO: 60 of at least 97%. In an embodiment, thepolypeptide has a sequence identity to SEQ ID NO: 60 of at least 98%. Inan embodiment, the polypeptide has a sequence identity to SEQ ID NO: 60of at least 99%.

In one embodiment, the polypeptides differ by up to 50 amino acids,e.g., between 1 and 50 amino acids, such as 1-45, 1-40, 1-35, 1-30,1-25, 1-20, 1-15, 1-10 or 1-5 amino acids, or 1, 2, 3, 4, 5, 6, 7, 8, 9,10, 11, 12, 13, 14, 15, 16, 17, 18, 19, 20, 21, 22, 23, 24, 25, 26, 27,28, 29, 30, 31, 32, 33, 34, 35, 36, 37, 38, 39, 40, 41, 42, 43, 44, 45,46, 47, 48, 49 or 50 amino acids from SEQ ID NO: 60. In one embodiment,the polypeptides differ by up to 50 amino acids, e.g., between 1 and 50amino acids, such as 1-45, 1-40, 1-35, 1-30, 1-25, 1-20, 1-15, 1-10 or1-5 amino acids, or 1, 2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, 15,16, 17, 18, 19, 20, 21, 22, 23, 24, 25, 26, 27, 28, 29, 30, 31, 32, 33,34, 35, 36, 37, 38, 39, 40, 41, 42, 43, 44, 45, 46, 47, 48, 49 or 50amino acids from SEQ ID NO: 63. In an embodiment, the polypeptide has atleast 60%, at least 70%, at least 75%, at least 80%, at least 85%, atleast 90%, at least 95%, or at least 100% of the activity of thepolypeptide of SEQ ID NO: 60.

In one embodiment, the polypeptide preferably comprises or consists ofthe amino acid sequence of SEQ ID NO: 59 and/or SEQ ID NO: 60 or anallelic variant thereof; comprises the amino acid sequence of SEQ ID NO:59 and/or SEQ ID NO: 60 and a N-terminal and/or C-terminal His-tagand/or HQ-tag; or is a fragment thereof having arabinofuranosidaseactivity and having at least 90% such as at least 91%, at least 92%, atleast 93%, at least 94%, at least 95%, at least 96%, at least 97%, atleast 98% or at least 99% of the length of the mature polypeptide. Inanother embodiment, the polypeptide comprises or consists of the maturepolypeptide of SEQ ID NO: 59. In another embodiment, the polypeptidecomprises or consists of the mature polypeptide of SEQ ID NO: 62. Inanother embodiment, the polypeptide comprises or consists of amino acids1 to 436 of SEQ ID NO: 59. In another embodiment, the polypeptidecomprises or consists of amino acids 1 to 436 of SEQ ID NO: 60. Inanother embodiment, the polypeptide comprises or consists of amino acids1 to 444 of SEQ ID NO: 62. In another embodiment, the polypeptidecomprises or consists of amino acids 1 to 444 of SEQ ID NO: 63. In anembodiment, the polypeptide has been isolated.

In a continuation of the ninth aspect, the invention relates to apolypeptide having arabinofuranosidase activity encoded by apolynucleotide that hybridizes under high stringency conditions or veryhigh stringency conditions with (i) the mature polypeptide codingsequence of SEQ ID NO: 58 or (ii) the full-length complement of (i). Inan embodiment, the polypeptide has been isolated.

In a continuation of the ninth aspect, the invention relates to apolypeptide having arabinofuranosidase activity encoded by apolynucleotide having a sequence identity to the mature polypeptidecoding sequence of SEQ ID NO: 58 or the cDNA sequence thereof of atleast 81%, e.g. at least 85%, at least 86%, at least 87%, at least 88%,at least 89%, at least 90%, at least 91%, at least 92%, at least 93%, atleast 94%, at least 95%, at least 96%, at least 97%, at least 98%, atleast 99%, or 100%. In a further embodiment, the polypeptide has beenisolated.

In a continuation of the ninth aspect, the invention relates to variantsof SEQ ID NO: 60 having arabinofuranosidase activity comprising,deletion, and/or insertion at one or more (e.g., several) positions. Inan embodiment, the number of positions comprising one or more amino acidsubstitutions, and/or one or more amino acid deletions, and/or one ormore amino acid insertions or any combination thereof in SEQ ID NO: 60is not more than 50, e.g., 1, 2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13,14, 15, 16, 17, 18, 19, 20, 21, 22, 23, 24, 25, 26, 27, 28, 29, 30, 31,32, 33, 34, 35, 36, 37, 38, 39, 40, 41, 42, 43, 44, 45, 46, 47, 48, 49or 50. In an embodiment, the number of positions comprising one or moreamino acid substitutions, and/or one or more amino acid deletions,and/or one or more amino acid insertions or any combination thereof inSEQ ID NO: 60 is not more than 10, e.g., 1, 2, 3, 4, 5, 6, 7, 8, 9 or10. In another embodiment, the number of substitutions, deletions,and/or insertions in SEQ ID NO: 60 is not more than 10, e.g., 1, 2, 3,4, 5, 6, 7, 8, 9 or 10. In a further embodiment, the number ofsubstitutions, preferably conservative substitutions, in SEQ ID NO: 60is not more than 10, e.g., 1, 2, 3, 4, 5, 6, 7, 8, 9 or 10. In anvariant, the polypeptide has at least 60%, at least 70%, at least 75%,at least 80%, at least 85%, at least 90%, at least 95%, or at least 100%of the activity of the polypeptide of SEQ ID NO: 60. Examples of aminoacid changes and conservative substitutions are described in the secondaspect of the invention.

In an embodiment, the polypeptide of the ninth aspect comprises themotif [H/Y][L/M]F[F/S][A/C/H/S/T/V][A/D/G/N/R]D[D/E/N]G (SEQ ID NO: 1),preferably the motif [H/Y]LF[F/S][A/S/V][A/D/G]DNG (SEQ ID NO: 2), morepreferable the motif YLFF[A/V][A/G]DNG (SEQ ID NO: 3), or even morepreferably the motif YLFFAGDNG (SEQ ID NO: 4).

In a tenth aspect, the invention relates to polypeptides havingarabinofuranosidase activity and having a sequence identity to themature polypeptide of SEQ ID NO: 65 of at least 84%, e.g., at least 85%,at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, atleast 91%, at least 92%, at least 93%, at least 94%, at least 95%, atleast 96%, at least 97%, at least 98%, at least 99%, which havearabinofuranosidase activity. In one embodiment, the polypeptides differby up to 48 amino acids, e.g., between 1 and 48 amino acids, such as1-45, 1-40, 1-35, 1-30, 1-25, 1-20, 1-15, 1-10 or 1-5 amino acids, or 1,2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, 15, 16, 17, 18, 19, 20, 21,22, 23, 24, 25, 26, 27, 28, 29, 30, 31, 32, 33, 34, 35, 36, 37, 38, 39,40, 41, 42, 43, 44, 45, 46, 47 or 48 amino acids from the maturepolypeptide of SEQ ID NO: 65.

In a continuation of the tenth aspect, the invention further relates topolypeptides having a sequence identity to SEQ ID NO: 66 of at least 84%which have arabinofuranosidase activity. In an embodiment, thepolypeptide has a sequence identity to SEQ ID NO: 66 of at least 86%. Inan embodiment, the polypeptide has a sequence identity to SEQ ID NO: 66of at least 87%. In an embodiment, the polypeptide has a sequenceidentity to SEQ ID NO: 66 of at least 88%. In an embodiment, thepolypeptide has a sequence identity to SEQ ID NO: 66 of at least 89%. Inan embodiment, the polypeptide has a sequence identity to SEQ ID NO: 66of at least 90%. In an embodiment, the polypeptide has a sequenceidentity to SEQ ID NO: 66 of at least 91%. In an embodiment, thepolypeptide has a sequence identity to SEQ ID NO: 66 of at least 92%. Inan embodiment, the polypeptide has a sequence identity to SEQ ID NO: 66of at least 93%. In an embodiment, the polypeptide has a sequenceidentity to SEQ ID NO: 66 of at least 94%. In an embodiment, thepolypeptide has a sequence identity to SEQ ID NO: 66 of at least 95%. Inan embodiment, the polypeptide has a sequence identity to SEQ ID NO: 66of at least 96%. In an embodiment, the polypeptide has a sequenceidentity to SEQ ID NO: 66 of at least 97%. In an embodiment, thepolypeptide has a sequence identity to SEQ ID NO: 66 of at least 98%. Inan embodiment, the polypeptide has a sequence identity to SEQ ID NO: 66of at least 99%.

In one embodiment, the polypeptides differ by up to 48 amino acids, suchas 1-45, 1-40, 1-35, 1-30, 1-25, 1-20, 1-15, 1-10 or 1-5 amino acids, or1, 2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, 15, 16, 17, 18, 19, 20,21, 22, 23, 24, 25, 26, 27, 28, 29, 30, 31, 32, 33, 34, 35, 36, 37, 38,39, 40, 41, 42, 43, 44, 45, 46, 47 or 48 amino acids from SEQ ID NO: 66.In one embodiment, the polypeptides differ by up to 48 amino acids, suchas 1-45, 1-40, 1-35, 1-30, 1-25, 1-20, 1-15, 1-10 or 1-5 amino acids, or1, 2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, 15, 16, 17, 18, 19, 20,21, 22, 23, 24, 25, 26, 27, 28, 29, 30, 31, 32, 33, 34, 35, 36, 37, 38,39, 40, 41, 42, 43, 44, 45, 46, 47 or 48 amino acids from SEQ ID NO: 69.In an embodiment, the polypeptide has at least 60%, at least 70%, atleast 75%, at least 80%, at least 85%, at least 90%, at least 95%, or atleast 100% of the activity of the polypeptide of SEQ ID NO: 66.

In one embodiment, the polypeptide preferably comprises or consists ofthe amino acid sequence of SEQ ID NO: 65 and/or SEQ ID NO: 66 or anallelic variant thereof; comprises the amino acid sequence of SEQ ID NO:65 and/or SEQ ID NO: 66 and a N-terminal and/or C-terminal His-tagand/or HQ-tag such as SEQ ID NO: 69; or is a fragment thereof havingarabinofuranosidase activity and having at least 90% such as at least91%, at least 92%, at least 93%, at least 94%, at least 95%, at least96%, at least 97%, at least 98% or at least 99% of the length of themature polypeptide. In another embodiment, the polypeptide comprises orconsists of the mature polypeptide of SEQ ID NO: 65. In anotherembodiment, the polypeptide comprises or consists of the maturepolypeptide of SEQ ID NO: 68. In another embodiment, the polypeptidecomprises or consists of amino acids 1 to 311 of SEQ ID NO: 65. Inanother embodiment, the polypeptide comprises or consists of amino acids1 to 311 of SEQ ID NO: 66. In another embodiment, the polypeptidecomprises or consists of amino acids 1 to 311 of SEQ ID NO: 68. Inanother embodiment, the polypeptide comprises or consists of amino acids1 to 311 of SEQ ID NO: 69. In an embodiment, the polypeptide has beenisolated.

In a continuation of the tenth aspect, the invention relates to apolypeptide having arabinofuranosidase activity encoded by apolynucleotide that hybridizes under high stringency conditions or veryhigh stringency conditions with (i) the mature polypeptide codingsequence of SEQ ID NO: 64 or (ii) the full-length complement of (i). Inan embodiment, the polypeptide has been isolated.

In a continuation of the tenth aspect, the invention relates to apolypeptide having arabinofuranosidase activity encoded by apolynucleotide having a sequence identity to the mature polypeptidecoding sequence of SEQ ID NO: 64 or the cDNA sequence thereof of atleast 84%, e.g., at least 85%, at least 86%, at least 87%, at least 88%,at least 89%, at least 90%, at least 91%, at least 92%, at least 93%, atleast 94%, at least 95%, at least 96%, at least 97%, at least 98%, atleast 99%, or 100%. In a further embodiment, the polypeptide has beenisolated.

In a continuation of the tenth aspect, the invention relates to variantsof SEQ ID NO: 66 having arabinofuranosidase activity comprising one ormore amino acid substitutions, and/or one or more amino acid deletions,and/or one or more amino acid insertions or any combination thereof atone or more (e.g., several) positions. In an embodiment, the number ofpositions comprising one or more amino acid substitutions, and/or one ormore amino acid deletions, and/or one or more amino acid insertions orany combination thereof in SEQ ID NO: 66 is not more than 48, e.g., 1,2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, 15, 16, 17, 18, 19, 20, 21,22, 23, 24, 25, 26, 27, 28, 29, 30, 31, 32, 33, 34, 35, 36, 37, 38, 39,40, 41, 42, 43, 44, 45, 46, 47 or 48. In an embodiment, the number ofpositions comprising one or more amino acid substitutions, and/or one ormore amino acid deletions, and/or one or more amino acid insertions orany combination thereof in SEQ ID NO: 66 is not more than 10, e.g., 1,2, 3, 4, 5, 6, 7, 8, 9 or 10. In another embodiment, the number ofsubstitutions, deletions, and/or insertions in SEQ ID NO: 66 is not morethan 10, e.g., 1, 2, 3, 4, 5, 6, 7, 8, 9 or 10. In a further embodiment,the number of substitutions, preferably conservative substitutions, inSEQ ID NO: 66 is not more than 10, e.g., 1, 2, 3, 4, 5, 6, 7, 8, 9 or10. In an embodiment, the variant has at least 60%, at least 70%, atleast 75%, at least 80%, at least 85%, at least 90%, at least 95%, or atleast 100% of the activity of the polypeptide of SEQ ID NO: 66. Examplesof amino acid changes and conservative substitutions are described inthe second aspect of the invention.

In an embodiment, the polypeptide of the tenth aspect comprises themotif [H/Y][L/M]F[F/S][A/C/H/S/T/V][A/D/G/N/R]D[D/E/N]G (SEQ ID NO: 1),preferably the motif [H/Y]LF[F/S][A/S/V][A/D/G]DNG (SEQ ID NO: 2), morepreferable the motif YLFF[A/V][A/G]DNG (SEQ ID NO: 3), or even morepreferably the motif YLFFAGDNG (SEQ ID NO: 4).

In an eleventh aspect, the invention relates to polypeptides havingarabinofuranosidase activity and having a sequence identity to themature polypeptide of SEQ ID NO: 104 of at least 87%, e.g., at least88%, at least 89%, at least 90%, at least 91%, at least 92%, at least93%, at least 94%, at least 95%, at least 96%, at least 97%, at least98%, at least 99%, which have arabinofuranosidase activity. In oneembodiment, the polypeptides differ by up to 39 amino acids, e.g.,between 1 and 39 amino acids, such as 1-35, 1-30, 1-25, 1-20, 1-15, 1-10or 1-5 amino acids, or 1, 2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13, 14,15, 16, 17, 18, 19, 20, 21, 22, 23, 24, 25, 26, 27, 28, 29, 30, 31, 32,33, 34, 35, 36, 37, 38 or 39 amino acids from the mature polypeptide ofSEQ ID NO: 104.

In a continuation of the eleventh aspect, the invention further relatesto polypeptides having a sequence identity to SEQ ID NO: 105 of at least87% which have arabinofuranosidase activity. In an embodiment, thepolypeptide has a sequence identity to SEQ ID NO: 105 of at least 88%.In an embodiment, the polypeptide has a sequence identity to SEQ ID NO:105 of at least 89%. In an embodiment, the polypeptide has a sequenceidentity to SEQ ID NO: 105 of at least 90%. In an embodiment, thepolypeptide has a sequence identity to SEQ ID NO: 105 of at least 91%.In an embodiment, the polypeptide has a sequence identity to SEQ ID NO:105 of at least 92%. In an embodiment, the polypeptide has a sequenceidentity to SEQ ID NO: 105 of at least 93%. In an embodiment, thepolypeptide has a sequence identity to SEQ ID NO: 105 of at least 94%.In an embodiment, the polypeptide has a sequence identity to SEQ ID NO:105 of at least 95%. In an embodiment, the polypeptide has a sequenceidentity to SEQ ID NO: 105 of at least 96%. In an embodiment, thepolypeptide has a sequence identity to SEQ ID NO: 105 of at least 97%.In an embodiment, the polypeptide has a sequence identity to SEQ ID NO:105 of at least 98%. In an embodiment, the polypeptide has a sequenceidentity to SEQ ID NO: 105 of at least 99%.

In one embodiment, the polypeptides differ by up to 39 amino acids,e.g., between 1 and 39 amino acids, such as 1-35, 1-30, 1-25, 1-20,1-15, 1-10 or 1-5 amino acids, or 1, 2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12,13, 14, 15, 16, 17, 18, 19, 20, 21, 22, 23, 24, 25, 26, 27, 28, 29, 30,31, 32, 33, 34, 35, 36, 37, 38 or 39 amino acids from SEQ ID NO: 105. Inan embodiment, the polypeptide has at least 60%, at least 70%, at least75%, at least 80%, at least 85%, at least 90%, at least 95%, or at least100% of the activity of the polypeptide of SEQ ID NO: 105.

In one embodiment, the polypeptide preferably comprises or consists ofthe amino acid sequence of SEQ ID NO: 104 and/or SEQ ID NO: 105 or anallelic variant thereof; comprises the amino acid sequence of SEQ ID NO:104 and/or SEQ ID NO: 105 and a N-terminal and/or C-terminal His-tagand/or HQ-tag; or is a fragment thereof having arabinofuranosidaseactivity and having at least 90% such as at least 91%, at least 92%, atleast 93%, at least 94%, at least 95%, at least 96%, at least 97%, atleast 98% or at least 99% of the length of the mature polypeptide. Inanother embodiment, the polypeptide comprises or consists of the maturepolypeptide of SEQ ID NO: 105. In another embodiment, the polypeptidecomprises or consists of amino acids 1 to 302 of SEQ ID NO: 104. Inanother embodiment, the polypeptide comprises or consists of amino acids1 to 302 of SEQ ID NO: 105. In an embodiment, the polypeptide has beenisolated.

In a continuation of the eleventh aspect, the invention relates to apolypeptide having arabinofuranosidase activity encoded by apolynucleotide that hybridizes under very high stringency conditionswith (i) the mature polypeptide coding sequence of SEQ ID NO: 103 or(ii) the full-length complement of (i). In an embodiment, thepolypeptide has been isolated.

In a continuation of the eleventh aspect, the invention relates to apolypeptide having arabinofuranosidase activity encoded by apolynucleotide having a sequence identity to the mature polypeptidecoding sequence of SEQ ID NO: 103 or the cDNA sequence thereof of atleast 87%, e.g., at least 88%, at least 89%, at least 90%, at least 91%,at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, atleast 97%, at least 98%, at least 99%, or 100%. In a further embodiment,the polypeptide has been isolated.

In a continuation of the eleventh aspect, the invention relates tovariants of SEQ ID NO: 105 having arabinofuranosidase activitycomprising one or more amino acid substitutions, and/or one or moreamino acid deletions, and/or one or more amino acid insertions or anycombination thereof at one or more (e.g., several) positions. In anembodiment, the number of positions comprising one or more amino acidsubstitutions, and/or one or more amino acid deletions, and/or one ormore amino acid insertions or any combination thereof in SEQ ID NO: 105is not more than 39, e.g., 1, 2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13,14, 15, 16, 17, 18, 19, 20, 21, 22, 23, 24, 25, 26, 27, 28, 29, 30, 31,32, 33, 34, 35, 36, 37, 38 or 39. In an embodiment, the number ofpositions comprising one or more amino acid substitutions, and/or one ormore amino acid deletions, and/or one or more amino acid insertions orany combination thereof in SEQ ID NO: 105 is not more than 10, e.g., 1,2, 3, 4, 5, 6, 7, 8, 9 or 10. In another embodiment, the number ofsubstitutions, deletions, and/or insertions in SEQ ID NO: 105 is notmore than 10, e.g., 1, 2, 3, 4, 5, 6, 7, 8, 9 or 10. In a furtherembodiment, the number of substitutions, preferably conservativesubstitutions, in SEQ ID NO: 105 is not more than 10, e.g., 1, 2, 3, 4,5, 6, 7, 8, 9 or 10. In an embodiment, the variant has at least 60%, atleast 70%, at least 75%, at least 80%, at least 85%, at least 90%, atleast 95%, or at least 100% of the activity of the polypeptide of SEQ IDNO: 105. Examples of amino acid changes and conservative substitutionsare described in the second aspect of the invention.

In an embodiment, the polypeptide of the eleventh aspect comprises themotif [H/Y][L/M]F[F/S][A/C/H/S/T/V][A/D/G/N/R]D[D/E/N]G (SEQ ID NO: 1),preferably the motif [H/Y]LF[F/S][A/S/V][A/D/G]DNG (SEQ ID NO: 2), morepreferable the motif YLFF[A/V][A/G]DNG (SEQ ID NO: 3), or even morepreferably the motif YLFFAGDNG (SEQ ID NO: 4).

In an twelfth aspect, the invention relates to polypeptides havingarabinofuranosidase activity and having a sequence identity to themature polypeptide of SEQ ID NO: 107 of at least 85%, e.g., at least90%, at least 91%, at least 92%, at least 93%, at least 94%, at least95%, at least 96%, at least 97%, at least 98%, at least 99%, which havearabinofuranosidase activity. In one embodiment, the polypeptides differby up to 50 amino acids, e.g., between 1 and 50 amino acids, such as1-45, 1-40, 1-35, 1-30, 1-25, 1-20, 1-15, 1-10 or 1-5 amino acids, or 1,2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, 15, 16, 17, 18, 19, 20, 21,22, 23, 24, 25, 26, 27, 28, 29, 30, 31, 32, 33, 34, 35, 36, 37, 38, 39,40, 41, 42, 43, 44, 45, 46, 47, 48, 49 or 50 amino acids from the maturepolypeptide of SEQ ID NO: 107.

In a continuation of the twelfth aspect, the invention further relatesto polypeptides having a sequence identity to SEQ ID NO: 108 of at least85% which have arabinofuranosidase activity. In an embodiment, thepolypeptide has a sequence identity to SEQ ID NO: 108 of at least 86%.In an embodiment, the polypeptide has a sequence identity to SEQ ID NO:108 of at least 87%. In an embodiment, the polypeptide has a sequenceidentity to SEQ ID NO: 108 of at least 88%. In an embodiment, thepolypeptide has a sequence identity to SEQ ID NO: 108 of at least 89%.In an embodiment, the polypeptide has a sequence identity to SEQ ID NO:108 of at least 90%. In an embodiment, the polypeptide has a sequenceidentity to SEQ ID NO: 108 of at least 91%. In an embodiment, thepolypeptide has a sequence identity to SEQ ID NO: 108 of at least 92%.In an embodiment, the polypeptide has a sequence identity to SEQ ID NO:108 of at least 93%. In an embodiment, the polypeptide has a sequenceidentity to SEQ ID NO: 108 of at least 94%. In an embodiment, thepolypeptide has a sequence identity to SEQ ID NO: 108 of at least 95%.In an embodiment, the polypeptide has a sequence identity to SEQ ID NO:108 of at least 96%. In an embodiment, the polypeptide has a sequenceidentity to SEQ ID NO: 108 of at least 97%. In an embodiment, thepolypeptide has a sequence identity to SEQ ID NO: 108 of at least 98%.In an embodiment, the polypeptide has a sequence identity to SEQ ID NO:108 of at least 99%.

In one embodiment, the polypeptides differ by up to 50 amino acids, suchas 1-45, 1-40, 1-35, 1-30, 1-25, 1-20, 1-15, 1-10 or 1-5 amino acids, or1, 2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, 15, 16, 17, 18, 19, 20,21, 22, 23, 24, 25, 26, 27, 28, 29, 30, 31, 32, 33, 34, 35, 36, 37, 38,39, 40, 41, 42, 43, 44, 45, 46, 47, 48, 49 or 50 amino acids from SEQ IDNO: 108. In one embodiment, the polypeptides differ by up to 50 aminoacids, such as 1-45, 1-40, 1-35, 1-30, 1-25, 1-20, 1-15, 1-10 or 1-5amino acids, or 1, 2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, 15, 16,17, 18, 19, 20, 21, 22, 23, 24, 25, 26, 27, 28, 29, 30, 31, 32, 33, 34,35, 36, 37, 38, 39, 40, 41, 42, 43, 44, 45, 46, 47, 48, 49 or 50 aminoacids from SEQ ID NO: 111. In an embodiment, the polypeptide has atleast 60%, at least 70%, at least 75%, at least 80%, at least 85%, atleast 90%, at least 95%, or at least 100% of the activity of thepolypeptide of SEQ ID NO: 108.

In one embodiment, the polypeptide preferably comprises or consists ofthe amino acid sequence of SEQ ID NO: 107 and/or SEQ ID NO: 108 or anallelic variant thereof; comprises the amino acid sequence of SEQ ID NO:107 and/or SEQ ID NO: 108 and a N-terminal and/or C-terminal His-tagand/or HQ-tag such as SEQ ID NO: 111; or is a fragment thereof havingarabinofuranosidase activity and having at least 90% such as at least91%, at least 92%, at least 93%, at least 94%, at least 95%, at least96%, at least 97%, at least 98% or at least 99% of the length of themature polypeptide. In another embodiment, the polypeptide comprises orconsists of the mature polypeptide of SEQ ID NO: 107. In anotherembodiment, the polypeptide comprises or consists of the maturepolypeptide of SEQ ID NO: 110. In another embodiment, the polypeptidecomprises or consists of amino acids 1 to 464 of SEQ ID NO: 107. Inanother embodiment, the polypeptide comprises or consists of amino acids1 to 464 of SEQ ID NO: 108. In another embodiment, the polypeptidecomprises or consists of amino acids 1 to 472 of SEQ ID NO: 110. Inanother embodiment, the polypeptide comprises or consists of amino acids1 to 472 of SEQ ID NO: 111. In an embodiment, the polypeptide has beenisolated.

In a continuation of the twelfth aspect, the invention relates to apolypeptide having arabinofuranosidase activity encoded by apolynucleotide that hybridizes under high stringency conditions or veryhigh stringency conditions with (i) the mature polypeptide codingsequence of SEQ ID NO: 106 or (ii) the full-length complement of (i). Inan embodiment, the polypeptide has been isolated.

In a continuation of the twelfth aspect, the invention relates to apolypeptide having arabinofuranosidase activity encoded by apolynucleotide having a sequence identity to the mature polypeptidecoding sequence of SEQ ID NO: 106 or the cDNA sequence thereof of atleast 85%, e.g., at least 90%, at least 91%, at least 92%, at least 93%,at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, atleast 99%, or 100%. In a further embodiment, the polypeptide has beenisolated.

In a continuation of the twelfth aspect, the invention relates tovariants of SEQ ID NO:

108 having arabinofuranosidase activity comprising one or more aminoacid substitutions, and/or one or more amino acid deletions, and/or oneor more amino acid insertions or any combination thereof at one or more(e.g., several) positions. In an embodiment, the number of positionscomprising one or more amino acid substitutions, and/or one or moreamino acid deletions, and/or one or more amino acid insertions or anycombination thereof in SEQ ID NO: 108 is not more than 50, e.g., 1, 2,3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, 15, 16, 17, 18, 19, 20, 21, 22,23, 24, 25, 26, 27, 28, 29, 30, 31, 32, 33, 34, 35, 36, 37, 38, 39, 40,41, 42, 43, 44, 45, 46, 47, 48, 49 or 50. In an embodiment, the numberof positions comprising one or more amino acid substitutions, and/or oneor more amino acid deletions, and/or one or more amino acid insertionsor any combination thereof in SEQ ID NO: 108 is not more than 10, e.g.,1, 2, 3, 4, 5, 6, 7, 8, 9 or 10. In another embodiment, the number ofsubstitutions, deletions, and/or insertions in SEQ ID NO: 108 is notmore than 10, e.g., 1, 2, 3, 4, 5, 6, 7, 8, 9 or 10. In a furtherembodiment, the number of substitutions, preferably conservativesubstitutions, in SEQ ID NO: 108 is not more than 10, e.g., 1, 2, 3, 4,5, 6, 7, 8, 9 or 10. In an embodiment, the variant has at least 60%, atleast 70%, at least 75%, at least 80%, at least 85%, at least 90%, atleast 95%, or at least 100% of the activity of the polypeptide of SEQ IDNO: 108. Examples of amino acid changes and conservative substitutionsare described in the second aspect of the invention.

In an embodiment, the polypeptide of the twelfth aspect comprises themotif [H/Y][L/M]F[F/S][A/C/H/S/T/V][A/D/G/N/R]D[D/E/N]G (SEQ ID NO: 1),preferably the motif [H/Y]LF[F/S][A/S/V][A/D/G]DNG (SEQ ID NO: 2), morepreferable the motif YLFF[A/V][A/G]DNG (SEQ ID NO: 3), or even morepreferably the motif YLFFAGDNG (SEQ ID NO: 4).

In a thirteenth aspect, the invention relates to polypeptides havingarabinofuranosidase activity and having a sequence identity to themature polypeptide of SEQ ID NO: 113 of at least 80%, e.g., at least85%, at least 86%, at least 87%, at least 88%, at least 89%, at least90%, at least 91%, at least 92%, at least 93%, at least 94%, at least95%, at least 96%, at least 97%, at least 98%, at least 99%, which havearabinofuranosidase activity. In one embodiment, the polypeptides differby up to 50 amino acids, e.g., between 1 and 50 amino acids, such as1-45, 1-40, 1-35, 1-30, 1-25, 1-20, 1-15, 1-10 or 1-5 amino acids, or 1,2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, 15, 16, 17, 18, 19, 20, 21,22, 23, 24, 25, 26, 27, 28, 29, 30, 31, 32, 33, 34, 35, 36, 37, 38, 39,40, 41, 42, 43, 44, 45, 46, 47, 48, 49 or 50 amino acids from the maturepolypeptide of SEQ ID NO: 113.

In a continuation of the thirteenth aspect, the invention furtherrelates to polypeptides having a sequence identity to SEQ ID NO: 114 ofat least 80% which have arabinofuranosidase activity. In an embodiment,the polypeptide has a sequence identity to SEQ ID NO: 114 of at least85%. In an embodiment, the polypeptide has a sequence identity to SEQ IDNO: 114 of at least 86%. In an embodiment, the polypeptide has asequence identity to SEQ ID NO: 114 of at least 87%. In an embodiment,the polypeptide has a sequence identity to SEQ ID NO: 114 of at least88%. In an embodiment, the polypeptide has a sequence identity to SEQ IDNO: 114 of at least 89%. In an embodiment, the polypeptide has asequence identity to SEQ ID NO: 114 of at least 90%. In an embodiment,the polypeptide has a sequence identity to SEQ ID NO: 114 of at least91%. In an embodiment, the polypeptide has a sequence identity to SEQ IDNO: 114 of at least 92%. In an embodiment, the polypeptide has asequence identity to SEQ ID NO: 114 of at least 93%. In an embodiment,the polypeptide has a sequence identity to SEQ ID NO: 114 of at least94%. In an embodiment, the polypeptide has a sequence identity to SEQ IDNO: 114 of at least 95%. In an embodiment, the polypeptide has asequence identity to SEQ ID NO: 114 of at least 96%. In an embodiment,the polypeptide has a sequence identity to SEQ ID NO: 114 of at least97%. In an embodiment, the polypeptide has a sequence identity to SEQ IDNO: 114 of at least 98%. In an embodiment, the polypeptide has asequence identity to SEQ ID NO: 114 of at least 99%.

In one embodiment, the polypeptides differ by up to 50 amino acids, suchas 1-45, 1-40, 1-35, 1-30, 1-25, 1-20, 1-15, 1-10 or 1-5 amino acids, or1, 2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, 15, 16, 17, 18, 19, 20,21, 22, 23, 24, 25, 26, 27, 28, 29, 30, 31, 32, 33, 34, 35, 36, 37, 38,39, 40, 41, 42, 43, 44, 45, 46, 47, 48, 49 or 50 amino acids from SEQ IDNO: 114. In one embodiment, the polypeptides differ by up to 50 aminoacids, such as 1-45, 1-40, 1-35, 1-30, 1-25, 1-20, 1-15, 1-10 or 1-5amino acids, or 1, 2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, 15, 16,17, 18, 19, 20, 21, 22, 23, 24, 25, 26, 27, 28, 29, 30, 31, 32, 33, 34,35, 36, 37, 38, 39, 40, 41, 42, 43, 44, 45, 46, 47, 48, 49 or 50 aminoacids from SEQ ID NO: 117. In an embodiment, the polypeptide has atleast 60%, at least 70%, at least 75%, at least 80%, at least 85%, atleast 90%, at least 95%, or at least 100% of the activity of thepolypeptide of SEQ ID NO: 114.

In one embodiment, the polypeptide preferably comprises or consists ofthe amino acid sequence of SEQ ID NO: 113 and/or SEQ ID NO: 114 or anallelic variant thereof; comprises the amino acid sequence of SEQ ID NO:113 and/or SEQ ID NO: 114 and a N-terminal and/or C-terminal His-tagand/or HQ-tag such as SEQ ID NO: 117; or is a fragment thereof havingarabinofuranosidase activity and having at least 90% such as at least91%, at least 92%, at least 93%, at least 94%, at least 95%, at least96%, at least 97%, at least 98% or at least 99% of the length of themature polypeptide. In another embodiment, the polypeptide comprises orconsists of the mature polypeptide of SEQ ID NO: 113. In anotherembodiment, the polypeptide comprises or consists of the maturepolypeptide of SEQ ID NO: 116. In another embodiment, the polypeptidecomprises or consists of amino acids 1 to 364 of SEQ ID NO: 113. Inanother embodiment, the polypeptide comprises or consists of amino acids1 to 364 of SEQ ID NO: 114. In another embodiment, the polypeptidecomprises or consists of amino acids 1 to 372 of SEQ ID NO: 116. Inanother embodiment, the polypeptide comprises or consists of amino acids1 to 372 of SEQ ID NO: 117. In an embodiment, the polypeptide has beenisolated.

In a continuation of the thirteenth aspect, the invention relates to apolypeptide having arabinofuranosidase activity encoded by apolynucleotide that hybridizes under high stringency conditions or veryhigh stringency conditions with (i) the mature polypeptide codingsequence of SEQ ID NO: 112 or (ii) the full-length complement of (i). Inan embodiment, the polypeptide has been isolated.

In a continuation of the thirteenth aspect, the invention relates to apolypeptide having arabinofuranosidase activity encoded by apolynucleotide having a sequence identity to the mature polypeptidecoding sequence of SEQ ID NO: 112 or the cDNA sequence thereof of atleast 80%, e.g., at least 85%, at least 86%, at least 87%, at least 88%,at least 89%, at least 90%, at least 91%, at least 92%, at least 93%, atleast 94%, at least 95%, at least 96%, at least 97%, at least 98%, atleast 99%, or 100%. In a further embodiment, the polypeptide has beenisolated.

In a continuation of the thirteenth aspect, the invention relates tovariants of SEQ ID NO: 114 having arabinofuranosidase activitycomprising one or more amino acid substitutions, and/or one or moreamino acid deletions, and/or one or more amino acid insertions or anycombination thereof at one or more (e.g., several) positions. In anembodiment, the number of positions comprising one or more amino acidsubstitutions, and/or one or more amino acid deletions, and/or one ormore amino acid insertions or any combination thereof in SEQ ID NO: 114is not more than 50, e.g., 1, 2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13,14, 15, 16, 17, 18, 19, 20, 21, 22, 23, 24, 25, 26, 27, 28, 29, 30, 31,32, 33, 34, 35, 36, 37, 38, 39, 40, 41, 42, 43, 44, 45, 46, 47, 48, 49or 50. In an embodiment, the number of positions comprising one or moreamino acid substitutions, and/or one or more amino acid deletions,and/or one or more amino acid insertions or any combination thereof inSEQ ID NO: 114 is not more than 10, e.g., 1, 2, 3, 4, 5, 6, 7, 8, 9 or10. In another embodiment, the number of substitutions, deletions,and/or insertions in SEQ ID NO: 114 is not more than 10, e.g., 1, 2, 3,4, 5, 6, 7, 8, 9 or 10. In a further embodiment, the number ofsubstitutions, preferably conservative substitutions, in SEQ ID NO: 114is not more than 10, e.g., 1, 2, 3, 4, 5, 6, 7, 8, 9 or 10. In anembodiment, the variant has at least 60%, at least 70%, at least 75%, atleast 80%, at least 85%, at least 90%, at least 95%, or at least 100% ofthe activity of the polypeptide of SEQ ID NO: 114. Examples of aminoacid changes and conservative substitutions are described in the secondaspect of the invention.

In an embodiment, the polypeptide of the thirteenth aspect comprises themotif [H/Y][L/M]F[F/S][A/C/H/S/T/V][A/D/G/N/R]D[D/E/N]G (SEQ ID NO: 1),preferably the motif [H/Y]LF[F/S][A/S/V][A/D/G]DNG (SEQ ID NO: 2), morepreferable the motif YLFF[A/V][A/G]DNG (SEQ ID NO: 3), or even morepreferably the motif YLFFAGDNG (SEQ ID NO: 4).

In a fourteenth aspect, the invention relates to polypeptides havingarabinofuranosidase activity and having a sequence identity to themature polypeptide of SEQ ID NO: 119 of at least 80%, e.g., at least85%, at least 86%, at least 87%, at least 88%, at least 89%, at least90%, at least 91%, at least 92%, at least 93%, at least 94%, at least95%, at least 96%, at least 97%, at least 98%, at least 99%, which havearabinofuranosidase activity. In one embodiment, the polypeptides differby up to 50 amino acids, e.g., between 1 and 50 amino acids, such as1-45, 1-40, 1-35, 1-30, 1-25, 1-20, 1-15, 1-10 or 1-5 amino acids, or 1,2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, 15, 16, 17, 18, 19, 20, 21,22, 23, 24, 25, 26, 27, 28, 29, 30, 31, 32, 33, 34, 35, 36, 37, 38, 39,40, 41, 42, 43, 44, 45, 46, 47, 48, 49 or 50 amino acids from the maturepolypeptide of SEQ ID NO: 119.

In a continuation of the fourteenth aspect, the invention furtherrelates to polypeptides having a sequence identity to SEQ ID NO: 120 ofat least 80% which have arabinofuranosidase activity. In an embodiment,the polypeptide has a sequence identity to SEQ ID NO: 120 of at least85%. In an embodiment, the polypeptide has a sequence identity to SEQ IDNO: 120 of at least 86%. In an embodiment, the polypeptide has asequence identity to SEQ ID NO: 120 of at least 87%. In an embodiment,the polypeptide has a sequence identity to SEQ ID NO: 120 of at least88%. In an embodiment, the polypeptide has a sequence identity to SEQ IDNO: 120 of at least 89%. In an embodiment, the polypeptide has asequence identity to SEQ ID NO: 120 of at least 90%. In an embodiment,the polypeptide has a sequence identity to SEQ ID NO: 120 of at least91%. In an embodiment, the polypeptide has a sequence identity to SEQ IDNO: 120 of at least 92%. In an embodiment, the polypeptide has asequence identity to SEQ ID NO: 120 of at least 93%. In an embodiment,the polypeptide has a sequence identity to SEQ ID NO: 120 of at least94%. In an embodiment, the polypeptide has a sequence identity to SEQ IDNO: 120 of at least 95%. In an embodiment, the polypeptide has asequence identity to SEQ ID NO: 120 of at least 96%. In an embodiment,the polypeptide has a sequence identity to SEQ ID NO: 120 of at least97%. In an embodiment, the polypeptide has a sequence identity to SEQ IDNO: 120 of at least 98%. In an embodiment, the polypeptide has asequence identity to SEQ ID NO: 120 of at least 99%.

In one embodiment, the polypeptides differ by up to 50 amino acids,e.g., between 1 and 50 amino acids, such as 1-45, 1-40, 1-35, 1-30,1-25, 1-20, 1-15, 1-10 or 1-5 amino acids, or 1, 2, 3, 4, 5, 6, 7, 8, 9,10, 11, 12, 13, 14, 15, 16, 17, 18, 19, 20, 21, 22, 23, 24, 25, 26, 27,28, 29, 30, 31, 32, 33, 34, 35, 36, 37, 38, 39, 40, 41, 42, 43, 44, 45,46, 47, 48, 49 or 50 amino acids from SEQ ID NO: 120. In an embodiment,the polypeptide has at least 60%, at least 70%, at least 75%, at least80%, at least 85%, at least 90%, at least 95%, or at least 100% of theactivity of the polypeptide of SEQ ID NO: 120.

In one embodiment, the polypeptide preferably comprises or consists ofthe amino acid sequence of SEQ ID NO: 119 and/or SEQ ID NO: 120 or anallelic variant thereof; comprises the amino acid sequence of SEQ ID NO:119 and/or SEQ ID NO: 120 and a N-terminal and/or C-terminal His-tagand/or HQ-tag; or is a fragment thereof having arabinofuranosidaseactivity and having at least 90% such as at least 91%, at least 92%, atleast 93%, at least 94%, at least 95%, at least 96%, at least 97%, atleast 98% or at least 99% of the length of the mature polypeptide. Inanother embodiment, the polypeptide comprises or consists of the maturepolypeptide of SEQ ID NO: 120. In another embodiment, the polypeptidecomprises or consists of amino acids 1 to 357 of SEQ ID NO: 119. Inanother embodiment, the polypeptide comprises or consists of amino acids1 to 357 of SEQ ID NO: 120. In an embodiment, the polypeptide has beenisolated.

In a continuation of the fourteenth aspect, the invention relates to apolypeptide having arabinofuranosidase activity encoded by apolynucleotide that hybridizes under high stringency conditions or veryhigh stringency conditions with (i) the mature polypeptide codingsequence of SEQ ID NO: 118 or (ii) the full-length complement of (i). Inan embodiment, the polypeptide has been isolated.

In a continuation of the fourteenth aspect, the invention relates to apolypeptide having arabinofuranosidase activity encoded by apolynucleotide having a sequence identity to the mature polypeptidecoding sequence of SEQ ID NO: 118 or the cDNA sequence thereof of atleast 80%, e.g., at least 85%, at least 86%, at least 87%, at least 88%,at least 89%, at least 90%, at least 91%, at least 92%, at least 93%, atleast 94%, at least 95%, at least 96%, at least 97%, at least 98%, atleast 99%, or 100%. In a further embodiment, the polypeptide has beenisolated.

In a continuation of the fourteenth aspect, the invention relates tovariants of SEQ ID NO: 120 having arabinofuranosidase activitycomprising one or more amino acid substitutions, and/or one or moreamino acid deletions, and/or one or more amino acid insertions or anycombination thereof at one or more (e.g., several) positions. In anembodiment, the number of positions comprising one or more amino acidsubstitutions, and/or one or more amino acid deletions, and/or one ormore amino acid insertions or any combination thereof in SEQ ID NO: 120is not more than 50, e.g., 1, 2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13,14, 15, 16, 17, 18, 19, 20, 21, 22, 23, 24, 25, 26, 27, 28, 29, 30, 31,32, 33, 34, 35, 36, 37, 38, 39, 40, 41, 42, 43, 44, 45, 46, 47, 48, 49or 50. In an embodiment, the number of positions comprising one or moreamino acid substitutions, and/or one or more amino acid deletions,and/or one or more amino acid insertions or any combination thereof inSEQ ID NO: 120 is not more than 10, e.g., 1, 2, 3, 4, 5, 6, 7, 8, 9 or10. In another embodiment, the number of substitutions, deletions,and/or insertions in SEQ ID NO: 120 is not more than 10, e.g., 1, 2, 3,4, 5, 6, 7, 8, 9 or 10. In a further embodiment, the number ofsubstitutions, preferably conservative substitutions, in SEQ ID NO: 120is not more than 10, e.g., 1, 2, 3, 4, 5, 6, 7, 8, 9 or 10. In anembodiment, the variant has at least 60%, at least 70%, at least 75%, atleast 80%, at least 85%, at least 90%, at least 95%, or at least 100% ofthe activity of the polypeptide of SEQ ID NO: 120. Examples of aminoacid changes and conservative substitutions are described in the secondaspect of the invention.

In an embodiment, the polypeptide of the fourteenth aspect comprises themotif [H/Y][L/M]F[F/S][A/C/H/S/T/V][A/D/G/N/R]D[D/E/N]G (SEQ ID NO: 1),preferably the motif [H/Y]LF[F/S][A/S/V][A/D/G]DNG (SEQ ID NO: 2), morepreferable the motif YLFF[A/V][A/G]DNG (SEQ ID NO: 3), or even morepreferably the motif YLFFAGDNG (SEQ ID NO: 4).

In a fifteenth aspect, the invention relates to polypeptides havingarabinofuranosidase activity and having a sequence identity to themature polypeptide of SEQ ID NO: 122 of at least 89%, e.g., at least90%, at least 91%, at least 92%, at least 93%, at least 94%, at least95%, at least 96%, at least 97%, at least 98%, at least 99%, which havearabinofuranosidase activity. In one embodiment, the polypeptides differby up to 33 amino acids, e.g., between 1 and 33 amino acids, such as1-30, 1-25, 1-20, 1-15, 1-10 or 1-5 amino acids, or 1, 2, 3, 4, 5, 6, 7,8, 9, 10, 11, 12, 13, 14, 15, 16, 17, 18, 19, 20, 21, 22, 23, 24, 25,26, 27, 28, 29, 30, 31, 32 or 33 amino acids from the mature polypeptideof SEQ ID NO: 122.

In a continuation of the fifteenth aspect, the invention further relatesto polypeptides having a sequence identity to SEQ ID NO: 123 of at least89% which have arabinofuranosidase activity. In an embodiment, thepolypeptide has a sequence identity to SEQ ID NO: 123 of at least 90%.In an embodiment, the polypeptide has a sequence identity to SEQ ID NO:123 of at least 91%. In an embodiment, the polypeptide has a sequenceidentity to SEQ ID NO: 123 of at least 92%. In an embodiment, thepolypeptide has a sequence identity to SEQ ID NO: 123 of at least 93%.In an embodiment, the polypeptide has a sequence identity to SEQ ID NO:123 of at least 94%. In an embodiment, the polypeptide has a sequenceidentity to SEQ ID NO: 123 of at least 95%. In an embodiment, thepolypeptide has a sequence identity to SEQ ID NO: 123 of at least 96%.In an embodiment, the polypeptide has a sequence identity to SEQ ID NO:123 of at least 97%. In an embodiment, the polypeptide has a sequenceidentity to SEQ ID NO: 123 of at least 98%. In an embodiment, thepolypeptide has a sequence identity to SEQ ID NO: 123 of at least 99%.

In one embodiment, the polypeptides differ by up to 50 amino acids,e.g., between 1 and 33 amino acids, such as 1-30, 1-25, 1-20, 1-15, 1-10or 1-5 amino acids, or 1, 2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13, 14,15, 16, 17, 18, 19, 20, 21, 22, 23, 24, 25, 26, 27, 28, 29, 30, 31, 32or 33 amino acids from SEQ ID NO: 123. In an embodiment, the polypeptidehas at least 60%, at least 70%, at least 75%, at least 80%, at least85%, at least 90%, at least 95%, or at least 100% of the activity of thepolypeptide of SEQ ID NO: 123.

In one embodiment, the polypeptide preferably comprises or consists ofthe amino acid sequence of SEQ ID NO: 122 and/or SEQ ID NO: 123 or anallelic variant thereof; comprises the amino acid sequence of SEQ ID NO:122 and/or SEQ ID NO: 123 and a N-terminal and/or C-terminal His-tagand/or HQ-tag; or is a fragment thereof having arabinofuranosidaseactivity and having at least 90% such as at least 91%, at least 92%, atleast 93%, at least 94%, at least 95%, at least 96%, at least 97%, atleast 98% or at least 99% of the length of the mature polypeptide. Inanother embodiment, the polypeptide comprises or consists of the maturepolypeptide of SEQ ID NO: 123. In another embodiment, the polypeptidecomprises or consists of amino acids 1 to 302 of SEQ ID NO: 122. Inanother embodiment, the polypeptide comprises or consists of amino acids1 to 302 of SEQ ID NO: 123. In an embodiment, the polypeptide has beenisolated.

In a continuation of the fifteenth aspect, the invention relates to apolypeptide having arabinofuranosidase activity encoded by apolynucleotide that hybridizes under high stringency conditions or veryhigh stringency conditions with (i) the mature polypeptide codingsequence of SEQ ID NO: 121 or (ii) the full-length complement of (i). Inan embodiment, the polypeptide has been isolated.

In a continuation of the fifteenth aspect, the invention relates to apolypeptide having arabinofuranosidase activity encoded by apolynucleotide having a sequence identity to the mature polypeptidecoding sequence of SEQ ID NO: 121 or the cDNA sequence thereof of atleast 89%, e.g., at least 90%, at least 91%, at least 92%, at least 93%,at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, atleast 99%, or 100%. In a further embodiment, the polypeptide has beenisolated.

In a continuation of the fifteenth aspect, the invention relates tovariants of SEQ ID NO: 123 having arabinofuranosidase activitycomprising one or more amino acid substitutions, and/or one or moreamino acid deletions, and/or one or more amino acid insertions or anycombination thereof at one or more (e.g., several) positions. In anembodiment, the number of positions comprising one or more amino acidsubstitutions, and/or one or more amino acid deletions, and/or one ormore amino acid insertions or any combination thereof in SEQ ID NO: 123is not more than 33, e.g., 1, 2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13,14, 15, 16, 17, 18, 19, 20, 21, 22, 23, 24, 25, 26, 27, 28, 29, 30, 31,32 or 33. In an embodiment, the number of positions comprising one ormore amino acid substitutions, and/or one or more amino acid deletions,and/or one or more amino acid insertions or any combination thereof inSEQ ID NO: 123 is not more than 10, e.g., 1, 2, 3, 4, 5, 6, 7, 8, 9 or10. In another embodiment, the number of substitutions, deletions,and/or insertions in SEQ ID NO: 123 is not more than 10, e.g., 1, 2, 3,4, 5, 6, 7, 8, 9 or 10. In a further embodiment, the number ofsubstitutions, preferably conservative substitutions, in SEQ ID NO: 123is not more than 10, e.g., 1, 2, 3, 4, 5, 6, 7, 8, 9 or 10. In anembodiment, the variant has at least 60%, at least 70%, at least 75%, atleast 80%, at least 85%, at least 90%, at least 95%, or at least 100% ofthe activity of the polypeptide of SEQ ID NO: 123. Examples of aminoacid changes and conservative substitutions are described in the secondaspect of the invention.

In an embodiment, the polypeptide of the fifteenth aspect comprises themotif [H/Y][L/M]F[F/S][A/C/H/S/T/V][A/D/G/N/R]D[D/E/N]G (SEQ ID NO: 1),preferably the motif [H/Y]LF[F/S][A/S/V][A/D/G]DNG (SEQ ID NO: 2), morepreferable the motif YLFF[A/V][A/G]DNG (SEQ ID NO: 3), or even morepreferably the motif YLFFAGDNG (SEQ ID NO: 4).

In a sixteenth aspect, the invention relates to polypeptides havingarabinofuranosidase activity and having a sequence identity to themature polypeptide of SEQ ID NO: 125 of at least 80%, e.g., at least85%, at least 86%, at least 87%, at least 88%, at least 89%, at least90%, at least 91%, at least 92%, at least 93%, at least 94%, at least95%, at least 96%, at least 97%, at least 98%, at least 99%, which havearabinofuranosidase activity. In one embodiment, the polypeptides differby up to 50 amino acids, e.g., between 1 and 50 amino acids, such as1-45, 1-40, 1-35, 1-30, 1-25, 1-20, 1-15, 1-10 or 1-5 amino acids, or 1,2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, 15, 16, 17, 18, 19, 20, 21,22, 23, 24, 25, 26, 27, 28, 29, 30, 31, 32, 33, 34, 35, 36, 37, 38, 39,40, 41, 42, 43, 44, 45, 46, 47, 48, 49 or 50 amino acids from the maturepolypeptide of SEQ ID NO: 125.

In a continuation of the sixteenth aspect, the invention further relatesto polypeptides having a sequence identity to SEQ ID NO: 126 of at least80% which have arabinofuranosidase activity. In an embodiment, thepolypeptide has a sequence identity to SEQ ID NO: 126 of at least 85%.In an embodiment, the polypeptide has a sequence identity to SEQ ID NO:126 of at least 86%. In an embodiment, the polypeptide has a sequenceidentity to SEQ ID NO: 126 of at least 87%. In an embodiment, thepolypeptide has a sequence identity to SEQ ID NO: 126 of at least 88%.In an embodiment, the polypeptide has a sequence identity to SEQ ID NO:126 of at least 89%. In an embodiment, the polypeptide has a sequenceidentity to SEQ ID NO: 126 of at least 90%. In an embodiment, thepolypeptide has a sequence identity to SEQ ID NO: 126 of at least 91%.In an embodiment, the polypeptide has a sequence identity to SEQ ID NO:126 of at least 92%. In an embodiment, the polypeptide has a sequenceidentity to SEQ ID NO: 126 of at least 93%. In an embodiment, thepolypeptide has a sequence identity to SEQ ID NO: 126 of at least 94%.In an embodiment, the polypeptide has a sequence identity to SEQ ID NO:126 of at least 95%. In an embodiment, the polypeptide has a sequenceidentity to SEQ ID NO: 126 of at least 96%. In an embodiment, thepolypeptide has a sequence identity to SEQ ID NO: 126 of at least 97%.In an embodiment, the polypeptide has a sequence identity to SEQ ID NO:126 of at least 98%. In an embodiment, the polypeptide has a sequenceidentity to SEQ ID NO: 126 of at least 99%.

In one embodiment, the polypeptides differ by up to 50 amino acids, suchas 1-45, 1-40, 1-35, 1-30, 1-25, 1-20, 1-15, 1-10 or 1-5 amino acids, or1, 2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, 15, 16, 17, 18, 19, 20,21, 22, 23, 24, 25, 26, 27, 28, 29, 30, 31, 32, 33, 34, 35, 36, 37, 38,39, 40, 41, 42, 43, 44, 45, 46, 47, 48, 49 or 50 amino acids from SEQ IDNO: 126. In one embodiment, the polypeptides differ by up to 50 aminoacids, such as 1-45, 1-40, 1-35, 1-30, 1-25, 1-20, 1-15, 1-10 or 1-5amino acids, or 1, 2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, 15, 16,17, 18, 19, 20, 21, 22, 23, 24, 25, 26, 27, 28, 29, 30, 31, 32, 33, 34,35, 36, 37, 38, 39, 40, 41, 42, 43, 44, 45, 46, 47, 48, 49 or 50 aminoacids from SEQ ID NO: 129. In an embodiment, the polypeptide has atleast 60%, at least 70%, at least 75%, at least 80%, at least 85%, atleast 90%, at least 95%, or at least 100% of the activity of thepolypeptide of SEQ ID NO: 126.

In one embodiment, the polypeptide preferably comprises or consists ofthe amino acid sequence of SEQ ID NO: 125 and/or SEQ ID NO: 126 or anallelic variant thereof; comprises the amino acid sequence of SEQ ID NO:125 and/or SEQ ID NO: 126 and a N-terminal and/or C-terminal His-tagand/or HQ-tag such as SEQ ID NO: 129; or is a fragment thereof havingarabinofuranosidase activity and having at least 90% such as at least91%, at least 92%, at least 93%, at least 94%, at least 95%, at least96%, at least 97%, at least 98% or at least 99% of the length of themature polypeptide. In another embodiment, the polypeptide comprises orconsists of the mature polypeptide of SEQ ID NO: 125. In anotherembodiment, the polypeptide comprises or consists of the maturepolypeptide of SEQ ID NO: 128. In another embodiment, the polypeptidecomprises or consists of amino acids 1 to 453 of SEQ ID NO: 125. Inanother embodiment, the polypeptide comprises or consists of amino acids1 to 453 of SEQ ID NO: 126. In another embodiment, the polypeptidecomprises or consists of amino acids 1 to 461 of SEQ ID NO: 128. Inanother embodiment, the polypeptide comprises or consists of amino acids1 to 461 of SEQ ID NO: 129. In an embodiment, the polypeptide has beenisolated.

In a continuation of the sixteenth aspect, the invention relates to apolypeptide having arabinofuranosidase activity encoded by apolynucleotide that hybridizes under high stringency conditions or veryhigh stringency conditions with (i) the mature polypeptide codingsequence of SEQ ID NO: 124 or (ii) the full-length complement of (i). Inan embodiment, the polypeptide has been isolated.

In a continuation of the sixteenth aspect, the invention relates to apolypeptide having arabinofuranosidase activity encoded by apolynucleotide having a sequence identity to the mature polypeptidecoding sequence of SEQ ID NO: 124 or the cDNA sequence thereof of atleast 80%, e.g., at least 85%, at least 86%, at least 87%, at least 88%,at least 89%, at least 90%, at least 91%, at least 92%, at least 93%, atleast 94%, at least 95%, at least 96%, at least 97%, at least 98%, atleast 99%, or 100%. In a further embodiment, the polypeptide has beenisolated.

In a continuation of the sixteenth aspect, the invention relates tovariants of SEQ ID NO: 126 having arabinofuranosidase activitycomprising one or more amino acid substitutions, and/or one or moreamino acid deletions, and/or one or more amino acid insertions or anycombination thereof at one or more (e.g., several) positions. In anembodiment, the number of positions comprising one or more amino acidsubstitutions, and/or one or more amino acid deletions, and/or one ormore amino acid insertions or any combination thereof in SEQ ID NO: 126is not more than 50, e.g., 1, 2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13,14, 15, 16, 17, 18, 19, 20, 21, 22, 23, 24, 25, 26, 27, 28, 29, 30, 31,32, 33, 34, 35, 36, 37, 38, 39, 40, 41, 42, 43, 44, 45, 46, 47, 48, 49or 50. In an embodiment, the number of positions comprising one or moreamino acid substitutions, and/or one or more amino acid deletions,and/or one or more amino acid insertions or any combination thereof inSEQ ID NO: 126 is not more than 10, e.g., 1, 2, 3, 4, 5, 6, 7, 8, 9 or10. In another embodiment, the number of substitutions, deletions,and/or insertions in SEQ ID NO: 126 is not more than 10, e.g., 1, 2, 3,4, 5, 6, 7, 8, 9 or 10. In a further embodiment, the number ofsubstitutions, preferably conservative substitutions, in SEQ ID NO: 126is not more than 10, e.g., 1, 2, 3, 4, 5, 6, 7, 8, 9 or 10. In anembodiment, the variant has at least 60%, at least 70%, at least 75%, atleast 80%, at least 85%, at least 90%, at least 95%, or at least 100% ofthe activity of the polypeptide of SEQ ID NO: 126. Examples of aminoacid changes and conservative substitutions are described in the secondaspect of the invention.

In an embodiment, the polypeptide of the sixteenth aspect comprises themotif [H/Y][L/M]F[F/S][A/C/H/S/T/V][A/D/G/N/R]D[D/E/N]G (SEQ ID NO: 1).

In a seventeenth aspect, the invention relates to polypeptides havingarabinofuranosidase activity and having a sequence identity to themature polypeptide of SEQ ID NO: 137 of at least 85%, e.g., at least86%, at least 87%, at least 88%, at least 89%, at least 90%, at least91%, at least 92%, at least 93%, at least 94%, at least 95%, at least96%, at least 97%, at least 98%, at least 99%, which havearabinofuranosidase activity. In one embodiment, the polypeptides differby up to 46 amino acids, e.g., between 1 and 46 amino acids, such as1-45, 1-40, 1-35, 1-30, 1-25, 1-20, 1-15, 1-10 or 1-5 amino acids, or 1,2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, 15, 16, 17, 18, 19, 20, 21,22, 23, 24, 25, 26, 27, 28, 29, 30, 31, 32, 33, 34, 35, 36, 37, 38, 39,40, 41, 42, 43, 44, 45 or 46 amino acids from the mature polypeptide ofSEQ ID NO: 137.

In a continuation of the seventeenth aspect, the invention furtherrelates to polypeptides having a sequence identity to SEQ ID NO: 138 ofat least 85% which have arabinofuranosidase activity. In an embodiment,the polypeptide has a sequence identity to SEQ ID NO: 138 of at least86%. In an embodiment, the polypeptide has a sequence identity to SEQ IDNO: 138 of at least 87%. In an embodiment, the polypeptide has asequence identity to SEQ ID NO: 138 of at least 88%. In an embodiment,the polypeptide has a sequence identity to SEQ ID NO: 138 of at least89%. In an embodiment, the polypeptide has a sequence identity to SEQ IDNO: 138 of at least 90%. In an embodiment, the polypeptide has asequence identity to SEQ ID NO: 138 of at least 91%. In an embodiment,the polypeptide has a sequence identity to SEQ ID NO: 138 of at least92%. In an embodiment, the polypeptide has a sequence identity to SEQ IDNO: 138 of at least 93%. In an embodiment, the polypeptide has asequence identity to SEQ ID NO: 138 of at least 94%. In an embodiment,the polypeptide has a sequence identity to SEQ ID NO: 138 of at least95%. In an embodiment, the polypeptide has a sequence identity to SEQ IDNO: 138 of at least 96%. In an embodiment, the polypeptide has asequence identity to SEQ ID NO: 138 of at least 97%. In an embodiment,the polypeptide has a sequence identity to SEQ ID NO: 138 of at least98%. In an embodiment, the polypeptide has a sequence identity to SEQ IDNO: 138 of at least 99%.

In one embodiment, the polypeptides differ by up to 46 amino acids,e.g., between 1 and 46 amino acids, such as 1-45, 1-40, 1-35, 1-30,1-25, 1-20, 1-15, 1-10 or 1-5 amino acids, or 1, 2, 3, 4, 5, 6, 7, 8, 9,10, 11, 12, 13, 14, 15, 16, 17, 18, 19, 20, 21, 22, 23, 24, 25, 26, 27,28, 29, 30, 31, 32, 33, 34, 35, 36, 37, 38, 39, 40, 41, 42, 43, 44, 45or 46 amino acids from SEQ ID NO: 138. In an embodiment, the polypeptidehas at least 60%, at least 70%, at least 75%, at least 80%, at least85%, at least 90%, at least 95%, or at least 100% of the activity of thepolypeptide of SEQ ID NO: 138.

In one embodiment, the polypeptide preferably comprises or consists ofthe amino acid sequence of SEQ ID NO: 137 and/or SEQ ID NO: 138 or anallelic variant thereof; comprises the amino acid sequence of SEQ ID NO:137 and/or SEQ ID NO: 138 and a N-terminal and/or C-terminal His-tagand/or HQ-tag; or is a fragment thereof having arabinofuranosidaseactivity and having at least 90% such as at least 91%, at least 92%, atleast 93%, at least 94%, at least 95%, at least 96%, at least 97%, atleast 98% or at least 99% of the length of the mature polypeptide. Inanother embodiment, the polypeptide comprises or consists of the maturepolypeptide of SEQ ID NO: 138. In another embodiment, the polypeptidecomprises or consists of amino acids 1 to 309 of SEQ ID NO: 137. Inanother embodiment, the polypeptide comprises or consists of amino acids1 to 309 of SEQ ID NO: 138. In an embodiment, the polypeptide has beenisolated.

In a continuation of the seventeenth aspect, the invention relates to apolypeptide having arabinofuranosidase activity encoded by apolynucleotide that hybridizes under high stringency conditions or veryhigh stringency conditions with (i) the mature polypeptide codingsequence of SEQ ID NO: 136 or (ii) the full-length complement of (i). Inan embodiment, the polypeptide has been isolated.

In a continuation of the seventeenth aspect, the invention relates to apolypeptide having arabinofuranosidase activity encoded by apolynucleotide having a sequence identity to the mature polypeptidecoding sequence of SEQ ID NO: 136 or the cDNA sequence thereof of atleast 85%, e.g., at least 86%, at least 87%, at least 88%, at least 89%,at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, atleast 95%, at least 96%, at least 97%, at least 98%, at least 99%, or100%. In a further embodiment, the polypeptide has been isolated.

In a continuation of the seventeenth aspect, the invention relates tovariants of SEQ ID NO: 138 having arabinofuranosidase activitycomprising one or more amino acid substitutions, and/or one or moreamino acid deletions, and/or one or more amino acid insertions or anycombination thereof at one or more (e.g., several) positions. In anembodiment, the number of positions comprising one or more amino acidsubstitutions, and/or one or more amino acid deletions, and/or one ormore amino acid insertions or any combination thereof in SEQ ID NO: 138is not more than 46, e.g., 1, 2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13,14, 15, 16, 17, 18, 19, 20, 21, 22, 23, 24, 25, 26, 27, 28, 29, 30, 31,32, 33, 34, 35, 36, 37, 38, 39, 40, 41, 42, 43, 44, 45, or 46. In anembodiment, the number of positions comprising one or more amino acidsubstitutions, and/or one or more amino acid deletions, and/or one ormore amino acid insertions or any combination thereof in SEQ ID NO: 138is not more than 10, e.g., 1, 2, 3, 4, 5, 6, 7, 8, 9 or 10. In anotherembodiment, the number of substitutions, deletions, and/or insertions inSEQ ID NO: 138 is not more than 10, e.g., 1, 2, 3, 4, 5, 6, 7, 8, 9 or10. In a further embodiment, the number of substitutions, preferablyconservative substitutions, in SEQ ID NO: 138 is not more than 10, e.g.,1, 2, 3, 4, 5, 6, 7, 8, 9 or 10. In an embodiment, the variant has atleast 60%, at least 70%, at least 75%, at least 80%, at least 85%, atleast 90%, at least 95%, or at least 100% of the activity of thepolypeptide of SEQ ID NO: 138. Examples of amino acid changes andconservative substitutions are described in the second aspect of theinvention.

In an embodiment, the polypeptide of the seventeenth aspect comprisesthe motif [H/Y][L/M]F[F/S][A/C/H/S/T/V][A/D/G/N/R]D[D/E/N]G (SEQ ID NO:1), preferably the motif [H/Y]LF[F/S][A/S/V][A/D/G]DNG (SEQ ID NO: 2),more preferable the motif YLFF[A/V][A/G]DNG (SEQ ID NO: 3), or even morepreferably the motif YLFFAGDNG (SEQ ID NO: 4).

In a eighteenth aspect, the invention relates to polypeptides havingarabinofuranosidase activity and having a sequence identity to themature polypeptide of SEQ ID NO: 140 of at least 89%, e.g., at least90%, at least 91%, at least 92%, at least 93%, at least 94%, at least95%, at least 96%, at least 97%, at least 98%, at least 99%, which havearabinofuranosidase activity. In one embodiment, the polypeptides differby up to 33 amino acids, e.g., between 1 and 33 amino acids, such as1-30, 1-25, 1-20, 1-15, 1-10 or 1-5 amino acids, or 1, 2, 3, 4, 5, 6, 7,8, 9, 10, 11, 12, 13, 14, 15, 16, 17, 18, 19, 20, 21, 22, 23, 24, 25,26, 27, 28, 29, 30, 31, 32 or 33 amino acids from the mature polypeptideof SEQ ID NO: 140.

In a continuation of the eighteenth aspect, the invention furtherrelates to polypeptides having a sequence identity to SEQ ID NO: 141 ofat least 89% which have arabinofuranosidase activity. In an embodiment,the polypeptide has a sequence identity to SEQ ID NO: 141 of at least90%. In an embodiment, the polypeptide has a sequence identity to SEQ IDNO: 141 of at least 91%. In an embodiment, the polypeptide has asequence identity to SEQ ID NO: 141 of at least 92%. In an embodiment,the polypeptide has a sequence identity to SEQ ID NO: 141 of at least93%. In an embodiment, the polypeptide has a sequence identity to SEQ IDNO: 141 of at least 94%. In an embodiment, the polypeptide has asequence identity to SEQ ID NO: 141 of at least 95%. In an embodiment,the polypeptide has a sequence identity to SEQ ID NO: 141 of at least96%. In an embodiment, the polypeptide has a sequence identity to SEQ IDNO: 141 of at least 97%. In an embodiment, the polypeptide has asequence identity to SEQ ID NO: 141 of at least 98%. In an embodiment,the polypeptide has a sequence identity to SEQ ID NO: 141 of at least99%.

In one embodiment, the polypeptides differ by up to 33 amino acids,e.g., between 1 and 33 amino acids, such as 1-30, 1-25, 1-20, 1-15, 1-10or 1-5 amino acids, or 1, 2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13, 14,15, 16, 17, 18, 19, 20, 21, 22, 23, 24, 25, 26, 27, 28, 29, 30, 31, 32or 33 amino acids from SEQ ID NO: 141. In one embodiment, thepolypeptides differ by up to 1 and 33 amino acids, such as 1-30, 1-25,1-20, 1-15, 1-10 or 1-5 amino acids, or 1, 2, 3, 4, 5, 6, 7, 8, 9, 10,11, 12, 13, 14, 15, 16, 17, 18, 19, 20, 21, 22, 23, 24, 25, 26, 27, 28,29, 30, 31, 32 or 33 amino acids from SEQ ID NO: 144. In an embodiment,the polypeptide has at least 60%, at least 70%, at least 75%, at least80%, at least 85%, at least 90%, at least 95%, or at least 100% of theactivity of the polypeptide of SEQ ID NO: 141.

In one embodiment, the polypeptide preferably comprises or consists ofthe amino acid sequence of SEQ ID NO: 140 and/or SEQ ID NO: 141 or anallelic variant thereof; comprises the amino acid sequence of SEQ ID NO:140 and/or SEQ ID NO: 141 and a N-terminal and/or C-terminal His-tagand/or HQ-tag such as SEQ ID NO: 144; or is a fragment thereof havingarabinofuranosidase activity and having at least 90% such as at least91%, at least 92%, at least 93%, at least 94%, at least 95%, at least96%, at least 97%, at least 98% or at least 99% of the length of themature polypeptide. In another embodiment, the polypeptide comprises orconsists of the mature polypeptide of SEQ ID NO: 140. In anotherembodiment, the polypeptide comprises or consists of the maturepolypeptide of SEQ ID NO: 143. In another embodiment, the polypeptidecomprises or consists of amino acids 1 to 304 of SEQ ID NO: 140. Inanother embodiment, the polypeptide comprises or consists of amino acids1 to 304 of SEQ ID NO: 141. In another embodiment, the polypeptidecomprises or consists of amino acids 1 to 312 of SEQ ID NO: 143. Inanother embodiment, the polypeptide comprises or consists of amino acids1 to 312 of SEQ ID NO: 144. In an embodiment, the polypeptide has beenisolated.

In a continuation of the eighteenth aspect, the invention relates to apolypeptide having arabinofuranosidase activity encoded by apolynucleotide that hybridizes under very high stringency conditionswith (i) the mature polypeptide coding sequence of SEQ ID NO: 139 or(ii) the full-length complement of (i). In an embodiment, thepolypeptide has been isolated.

In a continuation of the eighteenth aspect, the invention relates to apolypeptide having arabinofuranosidase activity encoded by apolynucleotide having a sequence identity to the mature polypeptidecoding sequence of SEQ ID NO: 139 or the cDNA sequence thereof of atleast 89%, e.g., at least 90%, at least 91%, at least 92%, at least 93%,at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, atleast 99%, or 100%. In a further embodiment, the polypeptide has beenisolated.

In a continuation of the eighteenth aspect, the invention relates tovariants of SEQ ID NO: 141 having arabinofuranosidase activitycomprising one or more amino acid substitutions, and/or one or moreamino acid deletions, and/or one or more amino acid insertions or anycombination thereof at one or more (e.g., several) positions. In anembodiment, the number of positions comprising one or more amino acidsubstitutions, and/or one or more amino acid deletions, and/or one ormore amino acid insertions or any combination thereof in SEQ ID NO: 141is not more than 33, e.g., 1, 2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13,14, 15, 16, 17, 18, 19, 20, 21, 22, 23, 24, 25, 26, 27, 28, 29, 30, 31,32 or 33. In an embodiment, the number of positions comprising one ormore amino acid substitutions, and/or one or more amino acid deletions,and/or one or more amino acid insertions or any combination thereof inSEQ ID NO: 141 is not more than 10, e.g., 1, 2, 3, 4, 5, 6, 7, 8, 9 or10. In another embodiment, the number of substitutions, deletions,and/or insertions in SEQ ID NO: 141 is not more than 10, e.g., 1, 2, 3,4, 5, 6, 7, 8, 9 or 10. In a further embodiment, the number ofsubstitutions, preferably conservative substitutions, in SEQ ID NO: 141is not more than 10, e.g., 1, 2, 3, 4, 5, 6, 7, 8, 9 or 10. In anembodiment, the variant has at least 60%, at least 70%, at least 75%, atleast 80%, at least 85%, at least 90%, at least 95%, or at least 100% ofthe activity of the polypeptide of SEQ ID NO: 141. Examples of aminoacid changes and conservative substitutions are described in the secondaspect of the invention.

In an embodiment, the polypeptide of the eighteenth aspect comprises themotif [H/Y][L/M]F[F/S][A/C/H/S/T/V][A/D/G/N/R]D[D/E/N]G (SEQ ID NO: 1),preferably the motif [H/Y]LF[F/S][A/S/V][A/D/G]DNG (SEQ ID NO: 2), morepreferable the motif YLFF[A/V][A/G]DNG (SEQ ID NO: 3), or even morepreferably the motif YLFFAGDNG (SEQ ID NO: 4).

In a nineteenth aspect, the invention relates to polypeptides havingarabinofuranosidase activity and having a sequence identity to themature polypeptide of SEQ ID NO: 146 of at least 86%, e.g., at least87%, at least 88%, at least 89%, at least 90%, at least 91%, at least92%, at least 93%, at least 94%, at least 95%, at least 96%, at least97%, at least 98%, at least 99%, which have arabinofuranosidaseactivity. In one embodiment, the polypeptides differ by up to 42 aminoacids, e.g., between 1 and 42 amino acids, such as 1-40, 1-35, 1-30,1-25, 1-20, 1-15, 1-10 or 1-5 amino acids, or 1, 2, 3, 4, 5, 6, 7, 8, 9,10, 11, 12, 13, 14, 15, 16, 17, 18, 19, 20, 21, 22, 23, 24, 25, 26, 27,28, 29, 30, 31, 32, 33, 34, 35, 36, 37, 38, 39, 40, 41 or 42 amino acidsfrom the mature polypeptide of SEQ ID NO: 146.

In a continuation of the nineteenth aspect, the invention furtherrelates to polypeptides having a sequence identity to SEQ ID NO: 147 ofat least 86% which have arabinofuranosidase activity. In an embodiment,the polypeptide has a sequence identity to SEQ ID NO: 147 of at least87%. In an embodiment, the polypeptide has a sequence identity to SEQ IDNO: 147 of at least 88%. In an embodiment, the polypeptide has asequence identity to SEQ ID NO: 147 of at least 89%. In an embodiment,the polypeptide has a sequence identity to SEQ ID NO: 147 of at least90%. In an embodiment, the polypeptide has a sequence identity to SEQ IDNO: 147 of at least 91%. In an embodiment, the polypeptide has asequence identity to SEQ ID NO: 147 of at least 92%. In an embodiment,the polypeptide has a sequence identity to SEQ ID NO: 147 of at least93%. In an embodiment, the polypeptide has a sequence identity to SEQ IDNO: 147 of at least 94%. In an embodiment, the polypeptide has asequence identity to SEQ ID NO: 147 of at least 95%. In an embodiment,the polypeptide has a sequence identity to SEQ ID NO: 147 of at least96%. In an embodiment, the polypeptide has a sequence identity to SEQ IDNO: 147 of at least 97%. In an embodiment, the polypeptide has asequence identity to SEQ ID NO: 147 of at least 98%. In an embodiment,the polypeptide has a sequence identity to SEQ ID NO: 147 of at least99%.

In one embodiment, the polypeptides differ by up to 42 amino acids,e.g., between 1 and 42 amino acids, such as 42 amino acids, such as1-40, 1-35, 1-30, 1-25, 1-20, 1-15, 1-10 or 1-5 amino acids, or 1, 2, 3,4, 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, 15, 16, 17, 18, 19, 20, 21, 22,23, 24, 25, 26, 27, 28, 29, 30, 31, 32, 33, 34, 35, 36, 37, 38, 39, 40,41 or 42 amino acids from SEQ ID NO: 147. In an embodiment, thepolypeptide has at least 60%, at least 70%, at least 75%, at least 80%,at least 85%, at least 90%, at least 95%, or at least 100% of theactivity of the polypeptide of SEQ ID NO: 147.

In one embodiment, the polypeptide preferably comprises or consists ofthe amino acid sequence of SEQ ID NO: 146 and/or SEQ ID NO: 147 or anallelic variant thereof; comprises the amino acid sequence of SEQ ID NO:146 and/or SEQ ID NO: 147 and a N-terminal and/or C-terminal His-tagand/or HQ-tag; or is a fragment thereof having arabinofuranosidaseactivity and having at least 90% such as at least 91%, at least 92%, atleast 93%, at least 94%, at least 95%, at least 96%, at least 97%, atleast 98% or at least 99% of the length of the mature polypeptide. Inanother embodiment, the polypeptide comprises or consists of the maturepolypeptide of SEQ ID NO: 147. In another embodiment, the polypeptidecomprises or consists of amino acids 1 to 302 of SEQ ID NO: 146. Inanother embodiment, the polypeptide comprises or consists of amino acids1 to 302 of SEQ ID NO: 147. In an embodiment, the polypeptide has beenisolated.

In a continuation of the nineteenth aspect, the invention relates to apolypeptide having arabinofuranosidase activity encoded by apolynucleotide that hybridizes under high stringency conditions or veryhigh stringency conditions with (i) the mature polypeptide codingsequence of SEQ ID NO: 145 or (ii) the full-length complement of (i). Inan embodiment, the polypeptide has been isolated.

In a continuation of the nineteenth aspect, the invention relates to apolypeptide having arabinofuranosidase activity encoded by apolynucleotide having a sequence identity to the mature polypeptidecoding sequence of SEQ ID NO: 145 or the cDNA sequence thereof of atleast 86%, e.g., at least 87%, at least 88%, at least 89%, at least 90%,at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, atleast 96%, at least 97%, at least 98%, at least 99%, or 100%. In afurther embodiment, the polypeptide has been isolated.

In a continuation of the nineteenth aspect, the invention relates tovariants of SEQ ID NO: 147 having arabinofuranosidase activitycomprising one or more amino acid substitutions, and/or one or moreamino acid deletions, and/or one or more amino acid insertions or anycombination thereof at one or more (e.g., several) positions. In anembodiment, the number of positions comprising one or more amino acidsubstitutions, and/or one or more amino acid deletions, and/or one ormore amino acid insertions or any combination thereof in SEQ ID NO: 147is not more than 42, e.g., 1, 2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13,14, 15, 16, 17, 18, 19, 20, 21, 22, 23, 24, 25, 26, 27, 28, 29, 30, 31,32, 33, 34, 35, 36, 37, 38, 39, 40, 41 or 42. In an embodiment, thenumber of positions comprising one or more amino acid substitutions,and/or one or more amino acid deletions, and/or one or more amino acidinsertions or any combination thereof in SEQ ID NO: 147 is not more than10, e.g., 1, 2, 3, 4, 5, 6, 7, 8, 9 or 10. In another embodiment, thenumber of substitutions, deletions, and/or insertions in SEQ ID NO: 147is not more than 10, e.g., 1, 2, 3, 4, 5, 6, 7, 8, 9 or 10. In a furtherembodiment, the number of substitutions, preferably conservativesubstitutions, in SEQ ID NO: 147 is not more than 10, e.g., 1, 2, 3, 4,5, 6, 7, 8, 9 or 10. In an embodiment, the variant has at least 60%, atleast 70%, at least 75%, at least 80%, at least 85%, at least 90%, atleast 95%, or at least 100% of the activity of the polypeptide of SEQ IDNO: 147. Examples of amino acid changes and conservative substitutionsare described in the second aspect of the invention.

In an embodiment, the polypeptide of the nineteenth aspect comprises themotif [H/Y][L/M]F[F/S][A/C/H/S/T/V][A/D/G/N/R]D[D/E/N]G (SEQ ID NO: 1),preferably the motif [H/Y]LF[F/S][A/S/V][A/D/G]DNG (SEQ ID NO: 2), morepreferable the motif YLFF[A/V][A/G]DNG (SEQ ID NO: 3), or even morepreferably the motif YLFFAGDNG (SEQ ID NO: 4).

In a twentieth aspect, the invention relates to polypeptides havingarabinofuranosidase activity and having a sequence identity to themature polypeptide of SEQ ID NO: 155 of at least 96.4%, e.g., at least96.7%, at least 97.0%, at least 97.3%, at least 97.6%, at least 97.9%,at least 98.2%, at least 98.5%, at least 98.8%, at least 91.1%, at least99.4%, at least 99.7% which have arabinofuranosidase activity. In oneembodiment, the polypeptides differ by up to 11 amino acids, e.g.,between 1 and 11 amino acids, such as 1, 2, 3, 4, 5, 6, 7, 8, 9, 10 or11 amino acids from the mature polypeptide of SEQ ID NO: 155. In anembodiment, the polypeptide has at least 60%, at least 70%, at least75%, at least 80%, at least 85%, at least 90%, at least 95%, or at least100% of the activity of the polypeptide of SEQ ID NO: 155.

In a continuation of the twentieth aspect, the invention further relatesto polypeptides having a sequence identity to SEQ ID NO: 156 of at least96.4% which have arabinofuranosidase activity. In an embodiment, thepolypeptide has a sequence identity to SEQ ID NO: 156 of at least 96.7%.In an embodiment, the polypeptide has a sequence identity to SEQ ID NO:156 of at least 97.0%. In an embodiment, the polypeptide has a sequenceidentity to SEQ ID NO: 156 of at least 97.3%. In an embodiment, thepolypeptide has a sequence identity to SEQ ID NO: 156 of at least 97.6%.In an embodiment, the polypeptide has a sequence identity to SEQ ID NO:156 of at least 97.9%. In an embodiment, the polypeptide has a sequenceidentity to SEQ ID NO: 156 of at least 98.2%. In an embodiment, thepolypeptide has a sequence identity to SEQ ID NO: 156 of at least 98.5%.In an embodiment, the polypeptide has a sequence identity to SEQ ID NO:156 of at least 98.8%. In an embodiment, the polypeptide has a sequenceidentity to SEQ ID NO: 156 of at least 99.1%. In an embodiment, thepolypeptide has a sequence identity to SEQ ID NO: 156 of at least 99.4%.In an embodiment, the polypeptide has a sequence identity to SEQ ID NO:156 of at least 99.7%.

In one embodiment, the polypeptides differ by up to 11 amino acids,e.g., between 1 and 11 amino acids, such as 1, 2, 3, 4, 5, 6, 7, 8, 9,10 or 11 amino acids from SEQ ID NO: 156.

In one embodiment, the polypeptide preferably comprises or consists ofthe amino acid sequence of SEQ ID NO: 155 and/or SEQ ID NO: 156 or anallelic variant thereof; comprises the amino acid sequence of SEQ ID NO:155 and/or SEQ ID NO: 156 and a N-terminal and/or C-terminal His-tagand/or HQ-tag; or is a fragment thereof having arabinofuranosidaseactivity and having at least 90% such as at least 91%, at least 92%, atleast 93%, at least 94%, at least 95%, at least 96%, at least 97%, atleast 98% or at least 99% of the length of the mature polypeptide. Inanother embodiment, the polypeptide comprises or consists of the maturepolypeptide of SEQ ID NO: 156. In another embodiment, the polypeptidecomprises or consists of amino acids 1 to 316 of SEQ ID NO: 155. Inanother embodiment, the polypeptide comprises or consists of amino acids1 to 316 of SEQ ID NO: 156. In an embodiment, the polypeptide has beenisolated.

In a continuation of the twentieth aspect, the invention relates to apolypeptide having arabinofuranosidase activity encoded by apolynucleotide that hybridizes under very high stringency conditionswith (i) the mature polypeptide coding sequence of SEQ ID NO: 154 or(ii) the full-length complement of (i). In an embodiment, thepolypeptide has been isolated.

In a continuation of the twentieth aspect, the invention relates to apolypeptide having arabinofuranosidase activity encoded by apolynucleotide having a sequence identity to the mature polypeptidecoding sequence of SEQ ID NO: 154 or the cDNA sequence thereof of atleast 96.4%, e.g., at least 96.7%, at least 97.0%, at least 97.3%, atleast 97.6%, at least 97.9%, at least 98.2%, at least 98.5%, at least98.8%, at least 91.1%, at least 99.4%, at least 99.7%, or 100%. In afurther embodiment, the polypeptide has been isolated.

In a continuation of the twentieth aspect, the invention relates tovariants of SEQ ID NO: 156 having arabinofuranosidase activitycomprising one or more amino acid substitutions, and/or one or moreamino acid deletions, and/or one or more amino acid insertions or anycombination thereof at one or more (e.g., several) positions. In anembodiment, the number of positions comprising one or more amino acidsubstitutions, and/or one or more amino acid deletions, and/or one ormore amino acid insertions or any combination thereof in SEQ ID NO: 156is not more than 10, e.g., 1, 2, 3, 4, 5, 6, 7, 8, 9 or 10. In anotherembodiment, the number of substitutions, deletions, and/or insertions inSEQ ID NO: 156 is not more than 10, e.g., 1, 2, 3, 4, 5, 6, 7, 8, 9 or10. In a further embodiment, the number of substitutions, preferablyconservative substitutions, in SEQ ID NO: 156 is not more than 10, e.g.,1, 2, 3, 4, 5, 6, 7, 8, 9 or 10. In an embodiment, the variant has atleast 60%, at least 70%, at least 75%, at least 80%, at least 85%, atleast 90%, at least 95%, or at least 100% of the activity of thepolypeptide of SEQ ID NO: 155. Examples of amino acid changes andconservative substitutions are described in the second aspect of theinvention.

In an embodiment, the polypeptide of the twentieth aspect comprises themotif [H/Y][L/M]F[F/S][A/C/H/S/T/V][A/D/G/N/R]D[D/E/N]G (SEQ ID NO: 1),preferably the motif [H/Y]LF[F/S][A/S/V][A/D/G]DNG (SEQ ID NO: 2), morepreferable the motif [H/Y]LFSSDDNG (SEQ ID NO: 5), or even morepreferably the motif YLFSSDDNG (SEQ ID NO: 6).

In a twenty-first aspect, the invention relates to polypeptides havingarabinofuranosidase activity and having a sequence identity to themature polypeptide of SEQ ID NO: 161 of at least 80%, e.g., at least85%, at least 86%, at least 87%, at least 88%, at least 89%, at least90%, at least 91%, at least 92%, at least 93%, at least 94%, at least95%, at least 96%, at least 97%, at least 98%, at least 99%, which havearabinofuranosidase activity. In one embodiment, the polypeptides differby up to 50 amino acids, e.g., between 1 and 50 amino acids, such as1-45, 1-40, 1-35, 1-30, 1-25, 1-20, 1-15, 1-10 or 1-5 amino acids, or 1,2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, 15, 16, 17, 18, 19, 20, 21,22, 23, 24, 25, 26, 27, 28, 29, 30, 31, 32, 33, 34, 35, 36, 37, 38, 39,40, 41, 42, 43, 44, 45, 46, 47, 48, 49 or 50 amino acids from the maturepolypeptide of SEQ ID NO: 161.

In a continuation of the twenty-first aspect, the invention furtherrelates to polypeptides having a sequence identity to SEQ ID NO: 162 ofat least 80% which have arabinofuranosidase activity. In an embodiment,the polypeptide has a sequence identity to SEQ ID NO: 162 of at least85%. In an embodiment, the polypeptide has a sequence identity to SEQ IDNO: 162 of at least 86%. In an embodiment, the polypeptide has asequence identity to SEQ ID NO: 162 of at least 87%. In an embodiment,the polypeptide has a sequence identity to SEQ ID NO: 162 of at least88%. In an embodiment, the polypeptide has a sequence identity to SEQ IDNO: 162 of at least 89%. In an embodiment, the polypeptide has asequence identity to SEQ ID NO: 162 of at least 90%. In an embodiment,the polypeptide has a sequence identity to SEQ ID NO: 162 of at least91%. In an embodiment, the polypeptide has a sequence identity to SEQ IDNO: 162 of at least 92%. In an embodiment, the polypeptide has asequence identity to SEQ ID NO: 162 of at least 93%. In an embodiment,the polypeptide has a sequence identity to SEQ ID NO: 162 of at least94%. In an embodiment, the polypeptide has a sequence identity to SEQ IDNO: 162 of at least 95%. In an embodiment, the polypeptide has asequence identity to SEQ ID NO: 162 of at least 96%. In an embodiment,the polypeptide has a sequence identity to SEQ ID NO: 162 of at least97%. In an embodiment, the polypeptide has a sequence identity to SEQ IDNO: 162 of at least 98%. In an embodiment, the polypeptide has asequence identity to SEQ ID NO: 162 of at least 99%.

In one embodiment, the polypeptides differ by up to 50 amino acids,e.g., between 1 and 50 amino acids, such as 1-45, 1-40, 1-35, 1-30,1-25, 1-20, 1-15, 1-10 or 1-5 amino acids, or 1, 2, 3, 4, 5, 6, 7, 8, 9,10, 11, 12, 13, 14, 15, 16, 17, 18, 19, 20, 21, 22, 23, 24, 25, 26, 27,28, 29, 30, 31, 32, 33, 34, 35, 36, 37, 38, 39, 40, 41, 42, 43, 44, 45,46, 47, 48, 49 or 50 amino acids from SEQ ID NO: 162. In an embodiment,the polypeptide has at least 60%, at least 70%, at least 75%, at least80%, at least 85%, at least 90%, at least 95%, or at least 100% of theactivity of the polypeptide of SEQ ID NO: 162.

In one embodiment, the polypeptide preferably comprises or consists ofthe amino acid sequence of SEQ ID NO: 161 and/or SEQ ID NO: 162 or anallelic variant thereof; comprises the amino acid sequence of SEQ ID NO:161 and/or SEQ ID NO: 162 and a N-terminal and/or C-terminal His-tagand/or HQ-tag; or is a fragment thereof having arabinofuranosidaseactivity and having at least 90% such as at least 91%, at least 92%, atleast 93%, at least 94%, at least 95%, at least 96%, at least 97%, atleast 98% or at least 99% of the length of the mature polypeptide. Inanother embodiment, the polypeptide comprises or consists of the maturepolypeptide of SEQ ID NO: 162. In another embodiment, the polypeptidecomprises or consists of amino acids 1 to 303 of SEQ ID NO: 161. Inanother embodiment, the polypeptide comprises or consists of amino acids1 to 303 of SEQ ID NO: 162. In an embodiment, the polypeptide has beenisolated.

In a continuation of the twenty-first aspect, the invention relates to apolypeptide having arabinofuranosidase activity encoded by apolynucleotide that hybridizes under high stringency conditions or veryhigh stringency conditions with (i) the mature polypeptide codingsequence of SEQ ID NO: 160 or (ii) the full-length complement of (i). Inan embodiment, the polypeptide has been isolated.

In a continuation of the twenty-first aspect, the invention relates to apolypeptide having arabinofuranosidase activity encoded by apolynucleotide having a sequence identity to the mature polypeptidecoding sequence of SEQ ID NO: 160 or the cDNA sequence thereof of atleast 80%, e.g., at least 85%, at least 86%, at least 87%, at least 88%,at least 89%, at least 90%, at least 91%, at least 92%, at least 93%, atleast 94%, at least 95%, at least 96%, at least 97%, at least 98%, atleast 99%, or 100%. In a further embodiment, the polypeptide has beenisolated.

In a continuation of the twenty-first aspect, the invention relates tovariants of SEQ ID NO: 162 having arabinofuranosidase activitycomprising one or more amino acid substitutions, and/or one or moreamino acid deletions, and/or one or more amino acid insertions or anycombination thereof at one or more (e.g., several) positions. In anembodiment, the number of positions comprising one or more amino acidsubstitutions, and/or one or more amino acid deletions, and/or one ormore amino acid insertions or any combination thereof in SEQ ID NO: 162is not more than 50, e.g., 1, 2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13,14, 15, 16, 17, 18, 19, 20, 21, 22, 23, 24, 25, 26, 27, 28, 29, 30, 31,32, 33, 34, 35, 36, 37, 38, 39, 40, 41, 42, 43, 44, 45, 46, 47, 48, 49or 50. In an embodiment, the number of positions comprising one or moreamino acid substitutions, and/or one or more amino acid deletions,and/or one or more amino acid insertions or any combination thereof inSEQ ID NO: 162 is not more than 10, e.g., 1, 2, 3, 4, 5, 6, 7, 8, 9 or10. In another embodiment, the number of substitutions, deletions,and/or insertions in SEQ ID NO: 162 is not more than 10, e.g., 1, 2, 3,4, 5, 6, 7, 8, 9 or 10. In a further embodiment, the number ofsubstitutions, preferably conservative substitutions, in SEQ ID NO: 162is not more than 10, e.g., 1, 2, 3, 4, 5, 6, 7, 8, 9 or 10. In anembodiment, the variant has at least 60%, at least 70%, at least 75%, atleast 80%, at least 85%, at least 90%, at least 95%, or at least 100% ofthe activity of the polypeptide of SEQ ID NO: 162. Examples of aminoacid changes and conservative substitutions are described in the secondaspect of the invention.

In an embodiment, the polypeptide of the twenty-first aspect comprisesthe motif [H/Y][L/M]F[F/S][A/C/H/S/T/V][A/D/G/N/R]D[D/E/N]G (SEQ ID NO:1), preferably the motif [H/Y]LF[F/S][A/S/V][A/D/G]DNG (SEQ ID NO: 2),more preferable the motif YLFF[A/V][A/G]DNG (SEQ ID NO: 3), or even morepreferably the motif YLFFAGDNG (SEQ ID NO: 4).

In a twenty-second aspect, the invention relates to polypeptides havingarabinofuranosidase activity and having a sequence identity to themature polypeptide of SEQ ID NO: 164 of at least 80%, e.g., at least85%, at least 86%, at least 87%, at least 88%, at least 89%, at least90%, at least 91%, at least 92%, at least 93%, at least 94%, at least95%, at least 96%, at least 97%, at least 98%, at least 99%, which havearabinofuranosidase activity. In one embodiment, the polypeptides differby up to 50 amino acids, e.g., between 1 and 50 amino acids, such as1-45, 1-40, 1-35, 1-30, 1-25, 1-20, 1-15, 1-10 or 1-5 amino acids, or 1,2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, 15, 16, 17, 18, 19, 20, 21,22, 23, 24, 25, 26, 27, 28, 29, 30, 31, 32, 33, 34, 35, 36, 37, 38, 39,40, 41, 42, 43, 44, 45, 46, 47, 48, 49 or 50 amino acids from the maturepolypeptide of SEQ ID NO: 164.

In a continuation of the twenty-second aspect, the invention furtherrelates to polypeptides having a sequence identity to SEQ ID NO: 165 ofat least 80% which have arabinofuranosidase activity. In an embodiment,the polypeptide has a sequence identity to SEQ ID NO: 165 of at least85%. In an embodiment, the polypeptide has a sequence identity to SEQ IDNO: 165 of at least 86%. In an embodiment, the polypeptide has asequence identity to SEQ ID NO: 165 of at least 87%. In an embodiment,the polypeptide has a sequence identity to SEQ ID NO: 165 of at least88%. In an embodiment, the polypeptide has a sequence identity to SEQ IDNO: 165 of at least 89%. In an embodiment, the polypeptide has asequence identity to SEQ ID NO: 165 of at least 90%. In an embodiment,the polypeptide has a sequence identity to SEQ ID NO: 165 of at least91%. In an embodiment, the polypeptide has a sequence identity to SEQ IDNO: 165 of at least 92%. In an embodiment, the polypeptide has asequence identity to SEQ ID NO: 165 of at least 93%. In an embodiment,the polypeptide has a sequence identity to SEQ ID NO: 165 of at least94%. In an embodiment, the polypeptide has a sequence identity to SEQ IDNO: 165 of at least 95%. In an embodiment, the polypeptide has asequence identity to SEQ ID NO: 165 of at least 96%. In an embodiment,the polypeptide has a sequence identity to SEQ ID NO: 165 of at least97%. In an embodiment, the polypeptide has a sequence identity to SEQ IDNO: 165 of at least 98%. In an embodiment, the polypeptide has asequence identity to SEQ ID NO: 165 of at least 99%.

In one embodiment, the polypeptides differ by up to 50 amino acids,e.g., between 1 and 50 amino acids, such as 1-45, 1-40, 1-35, 1-30,1-25, 1-20, 1-15, 1-10 or 1-5 amino acids, or 1, 2, 3, 4, 5, 6, 7, 8, 9,10, 11, 12, 13, 14, 15, 16, 17, 18, 19, 20, 21, 22, 23, 24, 25, 26, 27,28, 29, 30, 31, 32, 33, 34, 35, 36, 37, 38, 39, 40, 41, 42, 43, 44, 45,46, 47, 48, 49 or 50 amino acids from SEQ ID NO: 165. In an embodiment,the polypeptide has at least 60%, at least 70%, at least 75%, at least80%, at least 85%, at least 90%, at least 95%, or at least 100% of theactivity of the polypeptide of SEQ ID NO: 165.

In one embodiment, the polypeptide preferably comprises or consists ofthe amino acid sequence of SEQ ID NO: 164 and/or SEQ ID NO: 165 or anallelic variant thereof; comprises the amino acid sequence of SEQ ID NO:164 and/or SEQ ID NO: 165 and a N-terminal and/or C-terminal His-tagand/or HQ-tag; or is a fragment thereof having arabinofuranosidaseactivity and having at least 90% such as at least 91%, at least 92%, atleast 93%, at least 94%, at least 95%, at least 96%, at least 97%, atleast 98% or at least 99% of the length of the mature polypeptide. Inanother embodiment, the polypeptide comprises or consists of the maturepolypeptide of SEQ ID NO: 165. In another embodiment, the polypeptidecomprises or consists of amino acids 1 to 361 of SEQ ID NO: 164. Inanother embodiment, the polypeptide comprises or consists of amino acids1 to 361 of SEQ ID NO: 165. In an embodiment, the polypeptide has beenisolated.

In a continuation of the twenty-second aspect, the invention relates toa polypeptide having arabinofuranosidase activity encoded by apolynucleotide that hybridizes under high stringency conditions or veryhigh stringency conditions with (i) the mature polypeptide codingsequence of SEQ ID NO: 163 or (ii) the full-length complement of (i). Inan embodiment, the polypeptide has been isolated.

In a continuation of the twenty-second aspect, the invention relates toa polypeptide having arabinofuranosidase activity encoded by apolynucleotide having a sequence identity to the mature polypeptidecoding sequence of SEQ ID NO: 163 or the cDNA sequence thereof of atleast 80%, e.g., at least 85%, at least 86%, at least 87%, at least 88%,at least 89%, at least 90%, at least 91%, at least 92%, at least 93%, atleast 94%, at least 95%, at least 96%, at least 97%, at least 98%, atleast 99%, or 100%. In a further embodiment, the polypeptide has beenisolated.

In a continuation of the twenty-second aspect, the invention relates tovariants of SEQ ID NO: 165 having arabinofuranosidase activitycomprising one or more amino acid substitutions, and/or one or moreamino acid deletions, and/or one or more amino acid insertions or anycombination thereof at one or more (e.g., several) positions. In anembodiment, the number of positions comprising one or more amino acidsubstitutions, and/or one or more amino acid deletions, and/or one ormore amino acid insertions or any combination thereof in SEQ ID NO: 165is not more than 50, e.g., 1, 2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13,14, 15, 16, 17, 18, 19, 20, 21, 22, 23, 24, 25, 26, 27, 28, 29, 30, 31,32, 33, 34, 35, 36, 37, 38, 39, 40, 41, 42, 43, 44, 45, 46, 47, 48, 49or 50. In an embodiment, the number of positions comprising one or moreamino acid substitutions, and/or one or more amino acid deletions,and/or one or more amino acid insertions or any combination thereof inSEQ ID NO: 165 is not more than 10, e.g., 1, 2, 3, 4, 5, 6, 7, 8, 9 or10. In another embodiment, the number of substitutions, deletions,and/or insertions in SEQ ID NO: 165 is not more than 10, e.g., 1, 2, 3,4, 5, 6, 7, 8, 9 or 10. In a further embodiment, the number ofsubstitutions, preferably conservative substitutions, in SEQ ID NO: 165is not more than 10, e.g., 1, 2, 3, 4, 5, 6, 7, 8, 9 or 10. In anembodiment, the variant has at least 60%, at least 70%, at least 75%, atleast 80%, at least 85%, at least 90%, at least 95%, or at least 100% ofthe activity of the polypeptide of SEQ ID NO: 165. Examples of aminoacid changes and conservative substitutions are described in the secondaspect of the invention.

In an embodiment, the polypeptide of the twenty-second aspect comprisesthe motif [H/Y][L/M]F[F/S][A/C/H/S/T/V][A/D/G/N/R]D[D/E/N]G (SEQ ID NO:1), preferably the motif [H/Y]LF[F/S][A/S/V][A/D/G]DNG (SEQ ID NO: 2),more preferable the motif YLFF[A/V][A/G]DNG (SEQ ID NO: 3), or even morepreferably the motif YLFFAGDNG (SEQ ID NO: 4).

In a twenty-third aspect, the invention relates to polypeptides havingarabinofuranosidase activity and having a sequence identity to themature polypeptide of SEQ ID NO: 167 of at least 80%, e.g., at least85%, at least 86%, at least 87%, at least 88%, at least 89%, at least90%, at least 91%, at least 92%, at least 93%, at least 94%, at least95%, at least 96%, at least 97%, at least 98%, at least 99%, which havearabinofuranosidase activity. In one embodiment, the polypeptides differby up to 50 amino acids, e.g., between 1 and 50 amino acids, such as1-45, 1-40, 1-35, 1-30, 1-25, 1-20, 1-15, 1-10 or 1-5 amino acids, or 1,2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, 15, 16, 17, 18, 19, 20, 21,22, 23, 24, 25, 26, 27, 28, 29, 30, 31, 32, 33, 34, 35, 36, 37, 38, 39,40, 41, 42, 43, 44, 45, 46, 47, 48, 49 or 50 amino acids from the maturepolypeptide of SEQ ID NO: 167.

In a continuation of the twenty-third aspect, the invention furtherrelates to polypeptides having a sequence identity to SEQ ID NO: 168 ofat least 80% which have arabinofuranosidase activity. In an embodiment,the polypeptide has a sequence identity to SEQ ID NO: 168 of at least85%. In an embodiment, the polypeptide has a sequence identity to SEQ IDNO: 168 of at least 86%. In an embodiment, the polypeptide has asequence identity to SEQ ID NO: 168 of at least 87%. In an embodiment,the polypeptide has a sequence identity to SEQ ID NO: 168 of at least88%. In an embodiment, the polypeptide has a sequence identity to SEQ IDNO: 168 of at least 89%. In an embodiment, the polypeptide has asequence identity to SEQ ID NO: 168 of at least 90%. In an embodiment,the polypeptide has a sequence identity to SEQ ID NO: 168 of at least91%. In an embodiment, the polypeptide has a sequence identity to SEQ IDNO: 168 of at least 92%. In an embodiment, the polypeptide has asequence identity to SEQ ID NO: 168 of at least 93%. In an embodiment,the polypeptide has a sequence identity to SEQ ID NO: 168 of at least94%. In an embodiment, the polypeptide has a sequence identity to SEQ IDNO: 168 of at least 95%. In an embodiment, the polypeptide has asequence identity to SEQ ID NO: 168 of at least 96%. In an embodiment,the polypeptide has a sequence identity to SEQ ID NO: 168 of at least97%. In an embodiment, the polypeptide has a sequence identity to SEQ IDNO: 168 of at least 98%. In an embodiment, the polypeptide has asequence identity to SEQ ID NO: 168 of at least 99%.

In one embodiment, the polypeptides differ by up to 50 amino acids,e.g., between 1 and 50 amino acids, such as 1-45, 1-40, 1-35, 1-30,1-25, 1-20, 1-15, 1-10 or 1-5 amino acids, or 1, 2, 3, 4, 5, 6, 7, 8, 9,10, 11, 12, 13, 14, 15, 16, 17, 18, 19, 20, 21, 22, 23, 24, 25, 26, 27,28, 29, 30, 31, 32, 33, 34, 35, 36, 37, 38, 39, 40, 41, 42, 43, 44, 45,46, 47, 48, 49 or 50 amino acids from SEQ ID NO: 168. In an embodiment,the polypeptide has at least 60%, at least 70%, at least 75%, at least80%, at least 85%, at least 90%, at least 95%, or at least 100% of theactivity of the polypeptide of SEQ ID NO: 168.

In one embodiment, the polypeptide preferably comprises or consists ofthe amino acid sequence of SEQ ID NO: 167 and/or SEQ ID NO: 168 or anallelic variant thereof; comprises the amino acid sequence of SEQ ID NO:167 and/or SEQ ID NO: 168 and a N-terminal and/or C-terminal His-tagand/or HQ-tag; or is a fragment thereof having arabinofuranosidaseactivity and having at least 90% such as at least 91%, at least 92%, atleast 93%, at least 94%, at least 95%, at least 96%, at least 97%, atleast 98% or at least 99% of the length of the mature polypeptide. Inanother embodiment, the polypeptide comprises or consists of the maturepolypeptide of SEQ ID NO: 168. In another embodiment, the polypeptidecomprises or consists of amino acids 1 to 373 of SEQ ID NO: 167. Inanother embodiment, the polypeptide comprises or consists of amino acids1 to 373 of SEQ ID NO: 168. In an embodiment, the polypeptide has beenisolated.

In a continuation of the twenty-third aspect, the invention relates to apolypeptide having arabinofuranosidase activity encoded by apolynucleotide that hybridizes under high stringency conditions or veryhigh stringency conditions with (i) the mature polypeptide codingsequence of SEQ ID NO: 166 or (ii) the full-length complement of (i). Inan embodiment, the polypeptide has been isolated.

In a continuation of the twenty-third aspect, the invention relates to apolypeptide having arabinofuranosidase activity encoded by apolynucleotide having a sequence identity to the mature polypeptidecoding sequence of SEQ ID NO: 166 or the cDNA sequence thereof of atleast 80%, e.g., at least 85%, at least 86%, at least 87%, at least 88%,at least 89%, at least 90%, at least 91%, at least 92%, at least 93%, atleast 94%, at least 95%, at least 96%, at least 97%, at least 98%, atleast 99%, or 100%. In a further embodiment, the polypeptide has beenisolated.

In a continuation of the twenty-third aspect, the invention relates tovariants of SEQ ID NO: 168 having arabinofuranosidase activitycomprising one or more amino acid substitutions, and/or one or moreamino acid deletions, and/or one or more amino acid insertions or anycombination thereof at one or more (e.g., several) positions. In anembodiment, the number of positions comprising one or more amino acidsubstitutions, and/or one or more amino acid deletions, and/or one ormore amino acid insertions or any combination thereof in SEQ ID NO: 168is not more than 50, e.g., 1, 2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13,14, 15, 16, 17, 18, 19, 20, 21, 22, 23, 24, 25, 26, 27, 28, 29, 30, 31,32, 33, 34, 35, 36, 37, 38, 39, 40, 41, 42, 43, 44, 45, 46, 47, 48, 49or 50. In an embodiment, the number of positions comprising one or moreamino acid substitutions, and/or one or more amino acid deletions,and/or one or more amino acid insertions or any combination thereof inSEQ ID NO: 168 is not more than 10, e.g., 1, 2, 3, 4, 5, 6, 7, 8, 9 or10. In another embodiment, the number of substitutions, deletions,and/or insertions in SEQ ID NO: 168 is not more than 10, e.g., 1, 2, 3,4, 5, 6, 7, 8, 9 or 10. In a further embodiment, the number ofsubstitutions, preferably conservative substitutions, in SEQ ID NO: 168is not more than 10, e.g., 1, 2, 3, 4, 5, 6, 7, 8, 9 or 10. In anembodiment, the variant has at least 60%, at least 70%, at least 75%, atleast 80%, at least 85%, at least 90%, at least 95%, or at least 100% ofthe activity of the polypeptide of SEQ ID NO: 168. Examples of aminoacid changes and conservative substitutions are described in the secondaspect of the invention.

In an embodiment, the polypeptide of the twenty-third aspect comprisesthe motif [H/Y][L/M]F[F/S][A/C/H/S/T/V][A/D/G/N/R]D[D/E/N]G (SEQ ID NO:1), preferably the motif [H/Y]LF[F/S][A/S/V][A/D/G]DNG (SEQ ID NO: 2),more preferable the motif YLFF[A/V][A/G]DNG (SEQ ID NO: 3), or even morepreferably the motif YLFFAGDNG (SEQ ID NO: 4).

In a twenty-fourth aspect, the invention relates to polypeptides havingarabinofuranosidase activity and having a sequence identity to themature polypeptide of SEQ ID NO: 170 of at least 80%, e.g., at least85%, at least 86%, at least 87%, at least 88%, at least 89%, at least90%, at least 91%, at least 92%, at least 93%, at least 94%, at least95%, at least 96%, at least 97%, at least 98%, at least 99%, which havearabinofuranosidase activity. In one embodiment, the polypeptides differby up to 50 amino acids, e.g., between 1 and 50 amino acids, such as1-45, 1-40, 1-35, 1-30, 1-25, 1-20, 1-15, 1-10 or 1-5 amino acids, or 1,2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, 15, 16, 17, 18, 19, 20, 21,22, 23, 24, 25, 26, 27, 28, 29, 30, 31, 32, 33, 34, 35, 36, 37, 38, 39,40, 41, 42, 43, 44, 45, 46, 47, 48, 49 or 50 amino acids from the maturepolypeptide of SEQ ID NO: 170.

In a continuation of the twenty-fourth aspect, the invention furtherrelates to polypeptides having a sequence identity to SEQ ID NO: 171 ofat least 80% which have arabinofuranosidase activity. In an embodiment,the polypeptide has a sequence identity to SEQ ID NO: 171 of at least85%. In an embodiment, the polypeptide has a sequence identity to SEQ IDNO: 171 of at least 86%. In an embodiment, the polypeptide has asequence identity to SEQ ID NO: 171 of at least 87%. In an embodiment,the polypeptide has a sequence identity to SEQ ID NO: 171 of at least88%. In an embodiment, the polypeptide has a sequence identity to SEQ IDNO: 171 of at least 89%. In an embodiment, the polypeptide has asequence identity to SEQ ID NO: 171 of at least 90%. In an embodiment,the polypeptide has a sequence identity to SEQ ID NO: 171 of at least91%. In an embodiment, the polypeptide has a sequence identity to SEQ IDNO: 171 of at least 92%. In an embodiment, the polypeptide has asequence identity to SEQ ID NO: 171 of at least 93%. In an embodiment,the polypeptide has a sequence identity to SEQ ID NO: 171 of at least94%. In an embodiment, the polypeptide has a sequence identity to SEQ IDNO: 171 of at least 95%. In an embodiment, the polypeptide has asequence identity to SEQ ID NO: 171 of at least 96%. In an embodiment,the polypeptide has a sequence identity to SEQ ID NO: 171 of at least97%. In an embodiment, the polypeptide has a sequence identity to SEQ IDNO: 171 of at least 98%. In an embodiment, the polypeptide has asequence identity to SEQ ID NO: 171 of at least 99%.

In one embodiment, the polypeptides differ by up to 50 amino acids,e.g., between 1 and 50 amino acids, such as 1-45, 1-40, 1-35, 1-30,1-25, 1-20, 1-15, 1-10 or 1-5 amino acids, or 1, 2, 3, 4, 5, 6, 7, 8, 9,10, 11, 12, 13, 14, 15, 16, 17, 18, 19, 20, 21, 22, 23, 24, 25, 26, 27,28, 29, 30, 31, 32, 33, 34, 35, 36, 37, 38, 39, 40, 41, 42, 43, 44, 45,46, 47, 48, 49 or 50 amino acids from SEQ ID NO: 171. In an embodiment,the polypeptide has at least 60%, at least 70%, at least 75%, at least80%, at least 85%, at least 90%, at least 95%, or at least 100% of theactivity of the polypeptide of SEQ ID NO: 171.

In one embodiment, the polypeptide preferably comprises or consists ofthe amino acid sequence of SEQ ID NO: 170 and/or SEQ ID NO: 171 or anallelic variant thereof; comprises the amino acid sequence of SEQ ID NO:170 and/or SEQ ID NO: 171 and a N-terminal and/or C-terminal His-tagand/or HQ-tag; or is a fragment thereof having arabinofuranosidaseactivity and having at least 90% such as at least 91%, at least 92%, atleast 93%, at least 94%, at least 95%, at least 96%, at least 97%, atleast 98% or at least 99% of the length of the mature polypeptide. Inanother embodiment, the polypeptide comprises or consists of the maturepolypeptide of SEQ ID NO: 171. In another embodiment, the polypeptidecomprises or consists of amino acids 1 to 302 of SEQ ID NO: 170. Inanother embodiment, the polypeptide comprises or consists of amino acids1 to 302 of SEQ ID NO: 171. In an embodiment, the polypeptide has beenisolated.

In a continuation of the twenty-fourth aspect, the invention relates toa polypeptide having arabinofuranosidase activity encoded by apolynucleotide that hybridizes under high stringency conditions or veryhigh stringency conditions with (i) the mature polypeptide codingsequence of SEQ ID NO: 169 or (ii) the full-length complement of (i). Inan embodiment, the polypeptide has been isolated.

In a continuation of the twenty-fourth aspect, the invention relates toa polypeptide having arabinofuranosidase activity encoded by apolynucleotide having a sequence identity to the mature polypeptidecoding sequence of SEQ ID NO: 169 or the cDNA sequence thereof of atleast 80%, e.g., at least 85%, at least 86%, at least 87%, at least 88%,at least 89%, at least 90%, at least 91%, at least 92%, at least 93%, atleast 94%, at least 95%, at least 96%, at least 97%, at least 98%, atleast 99%, or 100%. In a further embodiment, the polypeptide has beenisolated.

In a continuation of the twenty-fourth aspect, the invention relates tovariants of SEQ ID NO: 171 having arabinofuranosidase activitycomprising one or more amino acid substitutions, and/or one or moreamino acid deletions, and/or one or more amino acid insertions or anycombination thereof at one or more (e.g., several) positions. In anembodiment, the number of positions comprising one or more amino acidsubstitutions, and/or one or more amino acid deletions, and/or one ormore amino acid insertions or any combination thereof in SEQ ID NO: 171is not more than 50, e.g., 1, 2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13,14, 15, 16, 17, 18, 19, 20, 21, 22, 23, 24, 25, 26, 27, 28, 29, 30, 31,32, 33, 34, 35, 36, 37, 38, 39, 40, 41, 42, 43, 44, 45, 46, 47, 48, 49or 50. In an embodiment, the number of positions comprising one or moreamino acid substitutions, and/or one or more amino acid deletions,and/or one or more amino acid insertions or any combination thereof inSEQ ID NO: 171 is not more than 10, e.g., 1, 2, 3, 4, 5, 6, 7, 8, 9 or10. In another embodiment, the number of substitutions, deletions,and/or insertions in SEQ ID NO: 171 is not more than 10, e.g., 1, 2, 3,4, 5, 6, 7, 8, 9 or 10. In a further embodiment, the number ofsubstitutions, preferably conservative substitutions, in SEQ ID NO: 171is not more than 10, e.g., 1, 2, 3, 4, 5, 6, 7, 8, 9 or 10. In anembodiment, the variant has at least 60%, at least 70%, at least 75%, atleast 80%, at least 85%, at least 90%, at least 95%, or at least 100% ofthe activity of the polypeptide of SEQ ID NO: 171. Examples of aminoacid changes and conservative substitutions are described in the secondaspect of the invention.

In an embodiment, the polypeptide of the twenty-fourth aspect comprisesthe motif [H/Y][L/M]F[F/S][A/C/H/S/T/V][A/D/G/N/R]D[D/E/N]G (SEQ ID NO:1), preferably the motif [H/Y]LF[F/S][A/S/V][A/D/G]DNG (SEQ ID NO: 2),more preferable the motif YLFF[A/V][A/G]DNG (SEQ ID NO: 3), or even morepreferably the motif YLFFAGDNG (SEQ ID NO: 4).

In a twenty-fifth aspect, the invention relates to polypeptides havingarabinofuranosidase activity and having a sequence identity to themature polypeptide of SEQ ID NO: 173 of at least 82%, e.g., at least85%, at least 86%, at least 87%, at least 88%, at least 89%, at least90%, at least 91%, at least 92%, at least 93%, at least 94%, at least95%, at least 96%, at least 97%, at least 98%, at least 99%, which havearabinofuranosidase activity. In one embodiment, the polypeptides differby up to 50 amino acids, e.g., between 1 and 50 amino acids, such as1-45, 1-40, 1-35, 1-30, 1-25, 1-20, 1-15, 1-10 or 1-5 amino acids, or 1,2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, 15, 16, 17, 18, 19, 20, 21,22, 23, 24, 25, 26, 27, 28, 29, 30, 31, 32, 33, 34, 35, 36, 37, 38, 39,40, 41, 42, 43, 44, 45, 46, 47, 48, 49 or 50 amino acids from the maturepolypeptide of SEQ ID NO: 173.

In a continuation of the twenty-fifth aspect, the invention furtherrelates to polypeptides having a sequence identity to SEQ ID NO: 174 ofat least 82% which have arabinofuranosidase activity. In an embodiment,the polypeptide has a sequence identity to SEQ ID NO: 174 of at least85%. In an embodiment, the polypeptide has a sequence identity to SEQ IDNO: 174 of at least 86%. In an embodiment, the polypeptide has asequence identity to SEQ ID NO: 174 of at least 87%. In an embodiment,the polypeptide has a sequence identity to SEQ ID NO: 174 of at least88%. In an embodiment, the polypeptide has a sequence identity to SEQ IDNO: 174 of at least 89%. In an embodiment, the polypeptide has asequence identity to SEQ ID NO: 174 of at least 90%. In an embodiment,the polypeptide has a sequence identity to SEQ ID NO: 174 of at least91%. In an embodiment, the polypeptide has a sequence identity to SEQ IDNO: 174 of at least 92%. In an embodiment, the polypeptide has asequence identity to SEQ ID NO: 174 of at least 93%. In an embodiment,the polypeptide has a sequence identity to SEQ ID NO: 174 of at least94%. In an embodiment, the polypeptide has a sequence identity to SEQ IDNO: 174 of at least 95%. In an embodiment, the polypeptide has asequence identity to SEQ ID NO: 174 of at least 96%. In an embodiment,the polypeptide has a sequence identity to SEQ ID NO: 174 of at least97%. In an embodiment, the polypeptide has a sequence identity to SEQ IDNO: 174 of at least 98%. In an embodiment, the polypeptide has asequence identity to SEQ ID NO: 174 of at least 99%.

In one embodiment, the polypeptides differ by up to 50 amino acids,e.g., between 1 and 50 amino acids, such as 1-45, 1-40, 1-35, 1-30,1-25, 1-20, 1-15, 1-10 or 1-5 amino acids, or 1, 2, 3, 4, 5, 6, 7, 8, 9,10, 11, 12, 13, 14, 15, 16, 17, 18, 19, 20, 21, 22, 23, 24, 25, 26, 27,28, 29, 30, 31, 32, 33, 34, 35, 36, 37, 38, 39, 40, 41, 42, 43, 44, 45,46, 47, 48, 49 or 50 amino acids from SEQ ID NO: 174. In an embodiment,the polypeptide has at least 60%, at least 70%, at least 75%, at least80%, at least 85%, at least 90%, at least 95%, or at least 100% of theactivity of the polypeptide of SEQ ID NO: 174.

In one embodiment, the polypeptide preferably comprises or consists ofthe amino acid sequence of SEQ ID NO: 173 and/or SEQ ID NO: 174 or anallelic variant thereof; comprises the amino acid sequence of SEQ ID NO:173 and/or SEQ ID NO: 174 and a N-terminal and/or C-terminal His-tagand/or HQ-tag; or is a fragment thereof having arabinofuranosidaseactivity and having at least 90% such as at least 91%, at least 92%, atleast 93%, at least 94%, at least 95%, at least 96%, at least 97%, atleast 98% or at least 99% of the length of the mature polypeptide. Inanother embodiment, the polypeptide comprises or consists of the maturepolypeptide of SEQ ID NO: 174. In another embodiment, the polypeptidecomprises or consists of amino acids 1 to 364 of SEQ ID NO: 173. Inanother embodiment, the polypeptide comprises or consists of amino acids1 to 364 of SEQ ID NO: 174. In an embodiment, the polypeptide has beenisolated.

In a continuation of the twenty-fifth aspect, the invention relates to apolypeptide having arabinofuranosidase activity encoded by apolynucleotide that hybridizes under high stringency conditions or veryhigh stringency conditions with (i) the mature polypeptide codingsequence of SEQ ID NO: 172 or (ii) the full-length complement of (i). Inan embodiment, the polypeptide has been isolated.

In a continuation of the twenty-fifth aspect, the invention relates to apolypeptide having arabinofuranosidase activity encoded by apolynucleotide having a sequence identity to the mature polypeptidecoding sequence of SEQ ID NO: 172 or the cDNA sequence thereof of atleast 82%, e.g., at least 85%, at least 86%, at least 87%, at least 88%,at least 89%, at least 90%, at least 91%, at least 92%, at least 93%, atleast 94%, at least 95%, at least 96%, at least 97%, at least 98%, atleast 99%, or 100%. In a further embodiment, the polypeptide has beenisolated.

In a continuation of the twenty-fifth aspect, the invention relates tovariants of SEQ ID NO: 174 having arabinofuranosidase activitycomprising one or more amino acid substitutions, and/or one or moreamino acid deletions, and/or one or more amino acid insertions or anycombination thereof at one or more (e.g., several) positions. In anembodiment, the number of positions comprising one or more amino acidsubstitutions, and/or one or more amino acid deletions, and/or one ormore amino acid insertions or any combination thereof in SEQ ID NO: 174is not more than 50, e.g., 1, 2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13,14, 15, 16, 17, 18, 19, 20, 21, 22, 23, 24, 25, 26, 27, 28, 29, 30, 31,32, 33, 34, 35, 36, 37, 38, 39, 40, 41, 42, 43, 44, 45, 46, 47, 48, 49or 50. In an embodiment, the number of positions comprising one or moreamino acid substitutions, and/or one or more amino acid deletions,and/or one or more amino acid insertions or any combination thereof inSEQ ID NO: 174 is not more than 10, e.g., 1, 2, 3, 4, 5, 6, 7, 8, 9 or10. In another embodiment, the number of substitutions, deletions,and/or insertions in SEQ ID NO: 174 is not more than 10, e.g., 1, 2, 3,4, 5, 6, 7, 8, 9 or 10. In a further embodiment, the number ofsubstitutions, preferably conservative substitutions, in SEQ ID NO: 174is not more than 10, e.g., 1, 2, 3, 4, 5, 6, 7, 8, 9 or 10. In anembodiment, the variant has at least 60%, at least 70%, at least 75%, atleast 80%, at least 85%, at least 90%, at least 95%, or at least 100% ofthe activity of the polypeptide of SEQ ID NO: 174. Examples of aminoacid changes and conservative substitutions are described in the secondaspect of the invention.

In an embodiment, the polypeptide of the twenty-fifth aspect comprisesthe motif [H/Y][L/M]F[F/S][A/C/H/S/T/V][A/D/G/N/R]D[D/E/N]G (SEQ ID NO:1), preferably the motif [H/Y]LF[F/S][A/S/V][A/D/G]DNG (SEQ ID NO: 2),more preferable the motif YLFF[A/V][A/G]DNG (SEQ ID NO: 3), or even morepreferably the motif YLFFAGDNG (SEQ ID NO: 4).

Polypeptides Having Xylanase Activity

In a twenty-sixth aspect, the invention relates to polypeptides havingxylanase activity and having a sequence identity to the maturepolypeptide of SEQ ID NO: 83 of at least 84%, e.g., at least 85%, atleast 86%, at least 87%, at least 88%, at least 89%, at least 90%, atleast 91%, at least 92%, at least 93%, at least 94%, at least 95%, atleast 96%, at least 97%, at least 98%, at least 99%, which have xylanaseactivity. In one embodiment, the polypeptides differ by up to 48 aminoacids, e.g., between 1 and 48 amino acids, such as 1-45, 1-40, 1-35,1-30, 1-25, 1-20, 1-15, 1-10 or 1-5 amino acids, or 1, 2, 3, 4, 5, 6, 7,8, 9, 10, 11, 12, 13, 14, 15, 16, 17, 18, 19, 20, 21, 22, 23, 24, 25,26, 27, 28, 29, 30, 31, 32, 33, 34, 35, 36, 37, 38, 39, 40, 41, 42, 43,44, 45, 46, 47 or 48 amino acids from the mature polypeptide of SEQ IDNO: 83.

In a continuation of the twenty-sixth aspect, the invention furtherrelates to polypeptides having a sequence identity to SEQ ID NO: 84 ofat least 84% which have xylanase activity. In an embodiment, thepolypeptide has a sequence identity to SEQ ID NO: 84 of at least 85%. Inan embodiment, the polypeptide has a sequence identity to SEQ ID NO: 84of at least 86%. In an embodiment, the polypeptide has a sequenceidentity to SEQ ID NO: 84 of at least 87%. In an embodiment, thepolypeptide has a sequence identity to SEQ ID NO: 84 of at least 88%. Inan embodiment, the polypeptide has a sequence identity to SEQ ID NO: 84of at least 89%. In an embodiment, the polypeptide has a sequenceidentity to SEQ ID NO: 84 of at least 90%. In an embodiment, thepolypeptide has a sequence identity to SEQ ID NO: 84 of at least 91%. Inan embodiment, the polypeptide has a sequence identity to SEQ ID NO: 84of at least 92%. In an embodiment, the polypeptide has a sequenceidentity to SEQ ID NO: 84 of at least 93%. In an embodiment, thepolypeptide has a sequence identity to SEQ ID NO: 84 of at least 94%. Inan embodiment, the polypeptide has a sequence identity to SEQ ID NO: 84of at least 95%. In an embodiment, the polypeptide has a sequenceidentity to SEQ ID NO: 84 of at least 96%. In an embodiment, thepolypeptide has a sequence identity to SEQ ID NO: 84 of at least 97%. Inan embodiment, the polypeptide has a sequence identity to SEQ ID NO: 84of at least 98%. In an embodiment, the polypeptide has a sequenceidentity to SEQ ID NO: 84 of at least 99%.

In one embodiment, the polypeptides differ by up to 48 amino acids,e.g., between 1 and 48 amino acids, such as 1-45, 1-40, 1-35, 1-30,1-25, 1-20, 1-15, 1-10 or 1-5 amino acids, or 1, 2, 3, 4, 5, 6, 7, 8, 9,10, 11, 12, 13, 14, 15, 16, 17, 18, 19, 20, 21, 22, 23, 24, 25, 26, 27,28, 29, 30, 31, 32, 33, 34, 35, 36, 37, 38, 39, 40, 41, 42, 43, 44, 45,46, 47 or 48 amino acids from SEQ ID NO: 84. In one embodiment, thepolypeptides differ by up to 48 amino acids, e.g., between 1 and 48amino acids, such as 1-45, 1-40, 1-35, 1-30, 1-25, 1-20, 1-15, 1-10 or1-5 amino acids, or 1, 2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, 15,16, 17, 18, 19, 20, 21, 22, 23, 24, 25, 26, 27, 28, 29, 30, 31, 32, 33,34, 35, 36, 37, 38, 39, 40, 41, 42, 43, 44, 45, 46, 47 or 48 amino acidsfrom SEQ ID NO: 87. In an embodiment, the polypeptide has at least 60%,at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, atleast 95%, or at least 100% of the activity of the polypeptide of SEQ IDNO: 84.

In one embodiment, the polypeptide preferably comprises or consists ofthe amino acid sequence of SEQ ID NO: 83 and/or SEQ ID NO: 84 or anallelic variant thereof; comprises the amino acid sequence of SEQ ID NO:84 and a N-terminal and/or C-terminal His-tag and/or HQ-tag such as SEQID NO: 86 and/or SEQ ID NO: 87; or is a fragment thereof having xylanaseactivity and having at least 90% such as at least 91%, at least 92%, atleast 93%, at least 94%, at least 95%, at least 96%, at least 97%, atleast 98% or at least 99% of the length of the mature polypeptide. Inanother embodiment, the polypeptide comprises or consists of the maturepolypeptide of SEQ ID NO: 83. In another embodiment, the polypeptidecomprises or consists of the mature polypeptide of SEQ ID NO: 86. Inanother embodiment, the polypeptide comprises or consists of amino acids1 to 299 of SEQ ID NO: 83. In another embodiment, the polypeptidecomprises or consists of amino acids 1 to 299 of SEQ ID NO: 84. Inanother embodiment, the polypeptide comprises or consists of amino acids1 to 307 of SEQ ID NO: 86. In another embodiment, the polypeptidecomprises or consists of amino acids 1 to 307 of SEQ ID NO: 87. In anembodiment, the polypeptide has been isolated.

In a continuation of the twenty-sixth aspect, the invention relates to apolypeptide having xylanase activity encoded by a polynucleotide thathybridizes under high stringency conditions or very high stringencyconditions with (i) the mature polypeptide coding sequence of SEQ ID NO:82 or (ii) the full-length complement of (i). In an embodiment, thepolypeptide has been isolated.

In a continuation of the twenty-sixth aspect, the invention relates to apolypeptide having xylanase activity encoded by a polynucleotide havinga sequence identity to the mature polypeptide coding sequence of SEQ IDNO: 82 or the cDNA sequence thereof of at least 84%, e.g., at least 85%,at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, atleast 91%, at least 92%, at least 93%, at least 94%, at least 95%, atleast 96%, at least 97%, at least 98%, at least 99%, or 100%. In afurther embodiment, the polypeptide has been isolated.

In a continuation of the twenty-sixth aspect, the invention relates tovariants of SEQ ID NO: 84 having xylanase activity comprising one ormore amino acid substitutions, and/or one or more amino acid deletions,and/or one or more amino acid insertions or any combination thereof atone or more (e.g., several) positions. In an embodiment, the number ofpositions comprising one or more amino acid substitutions, and/or one ormore amino acid deletions, and/or one or more amino acid insertions orany combination thereof in SEQ ID NO: 84 is not more than 48, e.g., 1,2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, 15, 16, 17, 18, 19, 20, 21,22, 23, 24, 25, 26, 27, 28, 29, 30, 31, 32, 33, 34, 35, 36, 37, 38, 39,40, 41, 42, 43, 44, 45, 46, 47 or 48. In another embodiment, the numberof positions comprising one or more amino acid substitutions, and/or oneor more amino acid deletions, and/or one or more amino acid insertionsor any combination thereof in SEQ ID NO: 84 is between 1 and 48, such as1-45, 1-40, 1-35, 1-30, 1-25, 1-20, 1-15, 1-10 or 1-5 positions. In anembodiment, the number of positions comprising one or more amino acidsubstitutions, and/or one or more amino acid deletions, and/or one ormore amino acid insertions or any combination thereof in SEQ ID NO: 84is not more than 10, e.g., 1, 2, 3, 4, 5, 6, 7, 8, 9 or 10. In anotherembodiment, the number of substitutions, deletions, and/or insertions inSEQ ID NO: 84 is not more than 10, e.g., 1, 2, 3, 4, 5, 6, 7, 8, 9 or10. In a further embodiment, the number of substitutions, preferablyconservative substitutions, in SEQ ID NO: 84 is not more than 10, e.g.,1, 2, 3, 4, 5, 6, 7, 8, 9 or 10. In an embodiment, the variant has atleast 60%, at least 70%, at least 75%, at least 80%, at least 85%, atleast 90%, at least 95%, or at least 100% of the activity of thepolypeptide of SEQ ID NO: 84. Examples of amino acid changes andconservative substitutions are described in the second aspect of theinvention.

In a twenty-seventh aspect, the invention relates to polypeptides havingxylanase activity and having a sequence identity to the maturepolypeptide of SEQ ID NO: 98 of at least 80%, e.g., at least 85%, atleast 86%, at least 87%, at least 88%, at least 89%, at least 90%, atleast 91%, at least 92%, at least 93%, at least 94%, at least 95%, atleast 96%, at least 97%, at least 98%, at least 99%, which have xylanaseactivity. In one embodiment, the polypeptides differ by up to 40 aminoacids, e.g., between 1 and 40 amino acids, such as 1-35, 1-30, 1-25,1-20, 1-15, 1-10 or 1-5 amino acids, or 1, 2, 3, 4, 5, 6, 7, 8, 9, 10,11, 12, 13, 14, 15, 16, 17, 18, 19, 20, 21, 22, 23, 24, 25, 26, 27, 28,29, 30, 31, 32, 33, 34, 35, 36, 37, 38, 39 or 40 amino acids from themature polypeptide of SEQ ID NO: 98.

In a continuation of the twenty-seventh aspect, the invention furtherrelates to polypeptides having a sequence identity to SEQ ID NO: 99 ofat least 80% which have xylanase activity. In an embodiment, thepolypeptide has a sequence identity to SEQ ID NO: 99 of at least 85%. Inan embodiment, the polypeptide has a sequence identity to SEQ ID NO: 99of at least 86%. In an embodiment, the polypeptide has a sequenceidentity to SEQ ID NO: 99 of at least 87%. In an embodiment, thepolypeptide has a sequence identity to SEQ ID NO: 99 of at least 88%. Inan embodiment, the polypeptide has a sequence identity to SEQ ID NO: 99of at least 89%. In an embodiment, the polypeptide has a sequenceidentity to SEQ ID NO: 99 of at least 90%. In an embodiment, thepolypeptide has a sequence identity to SEQ ID NO: 99 of at least 91%. Inan embodiment, the polypeptide has a sequence identity to SEQ ID NO: 99of at least 92%. In an embodiment, the polypeptide has a sequenceidentity to SEQ ID NO: 99 of at least 93%. In an embodiment, thepolypeptide has a sequence identity to SEQ ID NO: 99 of at least 94%. Inan embodiment, the polypeptide has a sequence identity to SEQ ID NO: 99of at least 95%. In an embodiment, the polypeptide has a sequenceidentity to SEQ ID NO: 99 of at least 96%. In an embodiment, thepolypeptide has a sequence identity to SEQ ID NO: 99 of at least 97%. Inan embodiment, the polypeptide has a sequence identity to SEQ ID NO: 99of at least 98%. In an embodiment, the polypeptide has a sequenceidentity to SEQ ID NO: 99 of at least 99%.

In one embodiment, the polypeptides differ by up to 40 amino acids,e.g., between 1 and 40 amino acids, such as 1-35, 1-30, 1-25, 1-20,1-15, 1-10 or 1-5 amino acids, or 1, 2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12,13, 14, 15, 16, 17, 18, 19, 20, 21, 22, 23, 24, 25, 26, 27, 28, 29, 30,31, 32, 33, 34, 35, 36, 37, 38, 39 or 40 amino acids from SEQ ID NO: 99.In an embodiment, the polypeptide has at least 60%, at least 70%, atleast 75%, at least 80%, at least 85%, at least 90%, at least 95%, or atleast 100% of the activity of the polypeptide of SEQ ID NO: 99.

In one embodiment, the polypeptide preferably comprises or consists ofthe amino acid sequence of SEQ ID NO: 98 and/or SEQ ID NO: 99 or anallelic variant thereof; comprises the amino acid sequence of SEQ ID NO:99 and a N-terminal and/or C-terminal His-tag and/or HQ-tag; or is afragment thereof having xylanase activity and having at least 90% suchas at least 91%, at least 92%, at least 93%, at least 94%, at least 95%,at least 96%, at least 97%, at least 98% or at least 99% of the lengthof the mature polypeptide. In another embodiment, the polypeptidecomprises or consists of the mature polypeptide of SEQ ID NO: 98. Inanother embodiment, the polypeptide comprises or consists of amino acids1 to 203 of SEQ ID NO: 98. In another embodiment, the polypeptidecomprises or consists of amino acids 1 to 203 of SEQ ID NO: 99. In anembodiment, the polypeptide has been isolated.

In a continuation of the twenty-seventh aspect, the invention relates toa polypeptide having xylanase activity encoded by a polynucleotide thathybridizes under high stringency conditions or very high stringencyconditions with (i) the mature polypeptide coding sequence of SEQ ID NO:97 or (ii) the full-length complement of (i). In an embodiment, thepolypeptide has been isolated.

In a continuation of the twenty-seventh aspect, the invention relates toa polypeptide having xylanase activity encoded by a polynucleotidehaving a sequence identity to the mature polypeptide coding sequence ofSEQ ID NO: 97 or the cDNA sequence thereof of at least 80%, e.g., atleast 85%, at least 86%, at least 87%, at least 88%, at least 89%, atleast 90%, at least 91%, at least 92%, at least 93%, at least 94%, atleast 95%, at least 96%, at least 97%, at least 98%, at least 99%, or100%. In a further embodiment, the polypeptide has been isolated.

In a continuation of the twenty-seventh aspect, the invention relates tovariants of SEQ ID NO: 99 having xylanase activity comprising one ormore amino acid substitutions, and/or one or more amino acid deletions,and/or one or more amino acid insertions or any combination thereof atone or more (e.g., several) positions. In an embodiment, the number ofpositions comprising one or more amino acid substitutions, and/or one ormore amino acid deletions, and/or one or more amino acid insertions orany combination thereof in SEQ ID NO: 99 is not more than 40, e.g., 1,2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, 15, 16, 17, 18, 19, 20, 21,22, 23, 24, 25, 26, 27, 28, 29, 30, 31, 32, 33, 34, 35, 36, 37, 38, 39or 40. In another embodiment, the number of positions comprising one ormore amino acid substitutions, and/or one or more amino acid deletions,and/or one or more amino acid insertions or any combination thereof inSEQ ID NO: 99 is between 1 and 48, such as 1-45, 1-40, 1-35, 1-30, 1-25,1-20, 1-15, 1-10 or 1-5 positions. In an embodiment, the number ofpositions comprising one or more amino acid substitutions, and/or one ormore amino acid deletions, and/or one or more amino acid insertions orany combination thereof in SEQ ID NO: 99 is not more than 10, e.g., 1,2, 3, 4, 5, 6, 7, 8, 9 or 10. In another embodiment, the number ofsubstitutions, deletions, and/or insertions in SEQ ID NO: 99 is not morethan 10, e.g., 1, 2, 3, 4, 5, 6, 7, 8, 9 or 10. In a further embodiment,the number of substitutions, preferably conservative substitutions, inSEQ ID NO: 99 is not more than 10, e.g., 1, 2, 3, 4, 5, 6, 7, 8, 9 or10. In an embodiment, the variant has at least 60%, at least 70%, atleast 75%, at least 80%, at least 85%, at least 90%, at least 95%, or atleast 100% of the activity of the polypeptide of SEQ ID NO: 99. Examplesof amino acid changes and conservative substitutions are described inthe second aspect of the invention.

In a twenty-eighth aspect, the invention relates to polypeptides havingxylanase activity and having a sequence identity to the maturepolypeptide of SEQ ID NO: 101 of at least 80%, e.g., at least 85%, atleast 86%, at least 87%, at least 88%, at least 89%, at least 90%, atleast 91%, at least 92%, at least 93%, at least 94%, at least 95%, atleast 96%, at least 97%, at least 98%, at least 99%, which have xylanaseactivity. In one embodiment, the polypeptides differ by up to 50 aminoacids, e.g., between 1 and 50 amino acids, such as 1-45, 1-40, 1-35,1-30, 1-25, 1-20, 1-15, 1-10 or 1-5 amino acids, or 1, 2, 3, 4, 5, 6, 7,8, 9, 10, 11, 12, 13, 14, 15, 16, 17, 18, 19, 20, 21, 22, 23, 24, 25,26, 27, 28, 29, 30, 31, 32, 33, 34, 35, 36, 37, 38, 39, 40, 41, 42, 43,44, 45, 46, 47, 48, 49 or 50 amino acids from the mature polypeptide ofSEQ ID NO: 101.

In a continuation of the twenty-eighth aspect, the invention furtherrelates to polypeptides having a sequence identity to SEQ ID NO: 102 ofat least 80% which have xylanase activity. In an embodiment, thepolypeptide has a sequence identity to SEQ ID NO: 102 of at least 85%.In an embodiment, the polypeptide has a sequence identity to SEQ ID NO:102 of at least 86%. In an embodiment, the polypeptide has a sequenceidentity to SEQ ID NO: 102 of at least 87%. In an embodiment, thepolypeptide has a sequence identity to SEQ ID NO: 102 of at least 88%.In an embodiment, the polypeptide has a sequence identity to SEQ ID NO:102 of at least 89%. In an embodiment, the polypeptide has a sequenceidentity to SEQ ID NO: 102 of at least 90%. In an embodiment, thepolypeptide has a sequence identity to SEQ ID NO: 102 of at least 91%.In an embodiment, the polypeptide has a sequence identity to SEQ ID NO:102 of at least 92%. In an embodiment, the polypeptide has a sequenceidentity to SEQ ID NO: 102 of at least 93%. In an embodiment, thepolypeptide has a sequence identity to SEQ ID NO: 102 of at least 94%.In an embodiment, the polypeptide has a sequence identity to SEQ ID NO:102 of at least 95%. In an embodiment, the polypeptide has a sequenceidentity to SEQ ID NO: 102 of at least 96%. In an embodiment, thepolypeptide has a sequence identity to SEQ ID NO: 102 of at least 97%.In an embodiment, the polypeptide has a sequence identity to SEQ ID NO:102 of at least 98%. In an embodiment, the polypeptide has a sequenceidentity to SEQ ID NO: 102 of at least 99%.

In one embodiment, the polypeptides differ by up to 50 amino acids,e.g., between 1 and 50 amino acids, such as 1-45, 1-40, 1-35, 1-30,1-25, 1-20, 1-15, 1-10 or 1-5 amino acids, or 1, 2, 3, 4, 5, 6, 7, 8, 9,10, 11, 12, 13, 14, 15, 16, 17, 18, 19, 20, 21, 22, 23, 24, 25, 26, 27,28, 29, 30, 31, 32, 33, 34, 35, 36, 37, 38, 39, 40, 41, 42, 43, 44, 45,46, 47, 48, 49 or 50 amino acids from SEQ ID NO: 102. In an embodiment,the polypeptide has at least 60%, at least 70%, at least 75%, at least80%, at least 85%, at least 90%, at least 95%, or at least 100% of theactivity of the polypeptide of SEQ ID NO: 102.

In one embodiment, the polypeptide preferably comprises or consists ofthe amino acid sequence of SEQ ID NO: 101 and/or SEQ ID NO: 102 or anallelic variant thereof; comprises the amino acid sequence of SEQ ID NO:102 and a N-terminal and/or C-terminal His-tag and/or HQ-tag; or is afragment thereof having xylanase activity and having at least 90% suchas at least 91%, at least 92%, at least 93%, at least 94%, at least 95%,at least 96%, at least 97%, at least 98% or at least 99% of the lengthof the mature polypeptide. In another embodiment, the polypeptidecomprises or consists of the mature polypeptide of SEQ ID NO: 101. Inanother embodiment, the polypeptide comprises or consists of amino acids1 to 203 of SEQ ID NO: 101. In another embodiment, the polypeptidecomprises or consists of amino acids 1 to 203 of SEQ ID NO: 102. In anembodiment, the polypeptide has been isolated.

In a continuation of the twenty-eighth aspect, the invention relates toa polypeptide having xylanase activity encoded by a polynucleotide thathybridizes under high stringency conditions or very high stringencyconditions with (i) the mature polypeptide coding sequence of SEQ ID NO:100 or (ii) the full-length complement of (i). In an embodiment, thepolypeptide has been isolated.

In a continuation of the twenty-eighth aspect, the invention relates toa polypeptide having xylanase activity encoded by a polynucleotidehaving a sequence identity to the mature polypeptide coding sequence ofSEQ ID NO: 100 or the cDNA sequence thereof of at least 80%, e.g., atleast 85%, at least 86%, at least 87%, at least 88%, at least 89%, atleast 90%, at least 91%, at least 92%, at least 93%, at least 94%, atleast 95%, at least 96%, at least 97%, at least 98%, at least 99%, or100%. In a further embodiment, the polypeptide has been isolated.

In a continuation of the twenty-eighth aspect, the invention relates tovariants of SEQ ID NO: 102 having xylanase activity comprising one ormore amino acid substitutions, and/or one or more amino acid deletions,and/or one or more amino acid insertions or any combination thereof atone or more (e.g., several) positions. In an embodiment, the number ofpositions comprising one or more amino acid substitutions, and/or one ormore amino acid deletions, and/or one or more amino acid insertions orany combination thereof in SEQ ID NO: 102 is not more than 40, e.g., 1,2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, 15, 16, 17, 18, 19, 20, 21,22, 23, 24, 25, 26, 27, 28, 29, 30, 31, 32, 33, 34, 35, 36, 37, 38, 39,40, 41, 42, 43, 44, 45, 46, 47, 48, 49 or 50. In another embodiment, thenumber of positions comprising one or more amino acid substitutions,and/or one or more amino acid deletions, and/or one or more amino acidinsertions or any combination thereof in SEQ ID NO: 102 is between 1 and48, such as 1-45, 1-40, 1-35, 1-30, 1-25, 1-20, 1-15, 1-10 or 1-5positions. In an embodiment, the number of positions comprising one ormore amino acid substitutions, and/or one or more amino acid deletions,and/or one or more amino acid insertions or any combination thereof inSEQ ID NO: 102 is not more than 10, e.g., 1, 2, 3, 4, 5, 6, 7, 8, 9 or10. In another embodiment, the number of substitutions, deletions,and/or insertions in SEQ ID NO: 102 is not more than 10, e.g., 1, 2, 3,4, 5, 6, 7, 8, 9 or 10. In a further embodiment, the number ofsubstitutions, preferably conservative substitutions, in SEQ ID NO: 102is not more than 10, e.g., 1, 2, 3, 4, 5, 6, 7, 8, 9 or 10. In anembodiment, the variant has at least 60%, at least 70%, at least 75%, atleast 80%, at least 85%, at least 90%, at least 95%, or at least 100% ofthe activity of the polypeptide of SEQ ID NO: 102. Examples of aminoacid changes and conservative substitutions are described in the secondaspect of the invention.

Sources of Polypeptides Having Arabinofuranosidase or Xylanase Activity

A polypeptide having arabinofuranosidase or xylanase activity of thepresent invention may be obtained from microorganisms of any genus. Forpurposes of the present invention, the term “obtained from” as usedherein in connection with a given source shall mean that the polypeptideencoded by a polynucleotide is produced by the source or by a strain inwhich the polynucleotide from the source has been inserted. In oneaspect, the polypeptide obtained from a given source is secretedextracellularly.

The polypeptide may be a fungal polypeptide. In one embodiment, thepolypeptide is from a fungus of the order Eurotiales, or from the familyAspergillaceae, or from the genus Penicillium or from the speciesPenicillium aurantiogriseum, Penicillium oxalicum, Penicilliumcapsulatum or Penicillium soppii.

In one embodiment, the polypeptide is from a fungus of the orderEurotiales, or from the family Aspergillaceae, or from the genusAspergillus or from the species Aspergillus clavatus, Aspergilluswentii, Aspergillus aculeatus or Aspergillus fumigatiaffinis.

In one embodiment, the polypeptide is from a fungus of the orderEurotiales, or from the family Aspergillaceae, or from the genusNeosartorya or from the species Neosartorya fischeri.

In one embodiment, the polypeptide is from a fungus of the orderEurotiales, or from the family Trichocomaceae, or from the genusTalaromyces or from the species Talaromyces pinophilus.

In one embodiment, the polypeptide is from a fungus of the orderUstilaginales, or from the family Ustilaginaceae, or from the genusUstilago or from the species Ustilago maydis.

In one embodiment, the polypeptide is from a fungus of the phylumAscomycota, or from the genus Acrophialophora or from the speciesAcrophialophora fusispora.

The polypeptide may be a bacterial polypeptide. In one embodiment, thepolypeptide is from a bacterium of the order Actinomycetales, or fromthe family Streptomycetaceae, or from the genus Streptomyces or from thespecies Streptomyces nitrosporeus or Streptomyces beijiangensis.

In one embodiment, the polypeptide is from a bacterium of the orderActinomycetales, or from the family Streptosporangiaceae, or from thegenus Streptosporangium or from the species Streptosporangium sp-60756.

In one embodiment, the polypeptide is from a fungus of the orderBotryosphaeriales, or from the family Botryosphaeriaceae, or from thegenus Lasiodiplodia or from the species Lasiodiplodia theobromae.

In one embodiment, the polypeptide is from a fungus of the orderPezizales, or from the family Ascobolaceae, or from the genus Ascobolusor from the species Ascobolus stictoideus.

In one embodiment, the polypeptide is from a fungus of the orderPleosporales, or from the family Pleosporaceae, or from the genusDrechslera or from the species Drechslera sp.

In one embodiment, the polypeptide is from a bacterium of the orderMicrococcales, or from the family Promicromonosporaceae, or from thegenus Xylanibacterium or from the species Xylanibacterium sp-61981.

In one embodiment, the polypeptide is from a fungus of the orderXylariales, or from the family Microdochiaceae, or from the genusMicrodochium or from the species Microdochium nivale.

In one embodiment, the polypeptide is from a fungus of the orderSordariales, or from the family Chaetomiaceae, or from the genusHumicola or from the species Humicola hyalothermophila or Humicola sp.

In one embodiment, the polypeptide is from a fungus of the orderPleosporales, or from the family Pleosporaceae, or from the genusCurvularia or from the species Curvularia geniculata.

In one embodiment, the polypeptide is from a bacterium of the orderGlycomycetales, or from the family Glycomycetaceae, or from the genusGlycomyces or from the species Glycomyces rutgersensis.

In one embodiment, the polypeptide is from a fungus of the orderSordariales, or from the genus Remersonia or from the species Remersoniathermophile.

In one embodiment, the polypeptide is from a fungus of the orderSordariales, or from the family Chaetomiaceae, or from the genusThielavia or from the species Thielavia arenaria or Thielavia terricola.

In one embodiment, the polypeptide is from a fungus of the orderSordariales, or from the family Chaetomiaceae, or from the genusChaetomium or from the species Chaetomium olivicolor.

It will be understood that for the aforementioned species, the inventionencompasses both the perfect and imperfect states, and other taxonomicequivalents, e.g., anamorphs, regardless of the species name by whichthey are known. Those skilled in the art will readily recognize theidentity of appropriate equivalents.

Strains of these species are readily accessible to the public in anumber of culture collections, such as the American Type CultureCollection (ATCC), Deutsche Sammlung von Mikroorganismen andZellkulturen GmbH (DSMZ), Centraalbureau Voor Schimmelcultures (CBS),and Agricultural Research Service Patent Culture Collection, NorthernRegional Research Center (NRRL).

The polypeptide may be identified and obtained from other sourcesincluding microorganisms isolated from nature (e.g., soil, composts,water, etc.) or DNA samples obtained directly from natural materials(e.g., soil, composts, water, etc.) using the above-mentioned probes.Techniques for isolating microorganisms and DNA directly from naturalhabitats are well known in the art. A polynucleotide encoding thepolypeptide may then be obtained by similarly screening a genomic DNA orcDNA library of another microorganism or mixed DNA sample. Once apolynucleotide encoding a polypeptide has been detected with theprobe(s), the polynucleotide can be isolated or cloned by utilizingtechniques that are known to those of ordinary skill in the art (see,e.g., Sambrook et al., 1989, supra).

Methods of Improving Animal Performance

In a twenty-ninth aspect, the invention relates to a method of improvingone or more performance parameters of an animal comprising administeringto one or more animals the composition of the first aspect of theinvention or any embodiment of the first aspect of the invention hereindefined, such as in the section related to ‘GH62 Polypeptides of theComposition’, or the section related to ‘GH10 and GH11 Polypeptides ofthe Composition’ or the section on ‘Combinations’ or as described in anyof the second to the twenty-eighth aspect of the invention. In anembodiment, the performance parameter is selected from the listconsisting of body weight gain, European Production Efficiency Factor(EPEF), European Production Efficacy Factor (EFF) and FCR.

The twenty-ninth aspect of the invention also relates to a method ofimproving one or more performance parameters of an animal comprisingadministering to one or more animals an animal feed additive comprisingthe composition of the first aspect of the invention or any embodimentof the first aspect of the invention herein defined (such as in thesection related to ‘GH62 Polypeptides of the Composition’, or thesection related to ‘GH10 and GH11 Polypeptides of the Composition’ orthe section on ‘Combinations’ or as described in any of the second tothe twenty-eighth aspect of the invention) and one or more formulatingagents. In an embodiment, the performance parameter is selected from thelist consisting of body weight gain, European Production EfficiencyFactor (EPEF), European Production Efficacy Factor (EFF) and FCR. In afurther embodiment, the animal feed additive comprises one or morecomponents selected from the list consisting of one or more additionalenzymes, one or more microbes, one or more vitamins, one or moreminerals, one or more amino acids, one or more other feed ingredients orany combination thereof.

The twenty-ninth aspect of the invention further relates to a method ofimproving one or more performance parameters of an animal comprisingadministering to one or more animals an animal feed comprising thecomposition of the first aspect of the invention or any embodiment ofthe first aspect of the invention herein defined (such as in the sectionrelated to ‘GH62 Polypeptides of the Composition’, or the sectionrelated to ‘GH10 and GH11 Polypeptides of the Composition’ or thesection on ‘Combinations’ or as described in any of the second to thetwenty-eighth aspect of the invention), one or more formulating agentsand plant based material from the sub-family Panicoideae. In anembodiment, the performance parameter is selected from the listconsisting of body weight gain, European Production Efficiency Factor(EPEF), European Production Efficacy Factor (EFF) and FCR. In a furtherembodiment, the animal feed additive comprises one or more componentsselected from the list consisting of one or more additional enzymes, oneor more microbes, one or more vitamins, one or more minerals, one ormore amino acids, one or more other feed ingredients or any combinationthereof.

The twenty-ninth aspect of the invention also relates to a method ofimproving one or more performance parameters of an animal comprisingadministering to one or more animals an animal feed additive comprisinga polypeptide having xylanase activity and having at least 80% sequenceidentity, e.g., at least 85%, at least 86%, at least 87%, at least 88%,at least 89%, at least 90%, at least 91%, at least 92%, at least 93%, atleast 94%, at least 95%, at least 96%, at least 97%, at least 98% or atleast 99% to the polypeptide of SEQ ID NO: 71. In one embodiment, thepolypeptides differ by up to 25 amino acids, e.g., between 1 and 25amino acids, such as 1-25, 1-20, 1-15, 1-10 or 1-5 amino acids, or 1, 2,3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, 15, 16, 17, 18, 19, 20, 21, 22,23, 24 or 25 amino acids from SEQ ID NO: 71. In one embodiment, thepolypeptide comprises or consists of the amino acid sequence of SEQ IDNO: 71; or is a fragment thereof having xylanase activity and having atleast 90% such as at least 91%, at least 92%, at least 93%, at least94%, at least 95%, at least 96%, at least 97%, at least 98% or at least99% of the length of the polypeptide. In another embodiment, polypeptidecomprises or consists of amino acids 1 to 288 of SEQ ID NO: 71.

The twenty-ninth aspect of the invention also relates to a method ofimproving one or more performance parameters of an animal comprisingadministering to one or more animals an animal feed additive comprisinga polypeptide having xylanase activity and having at least 80% sequenceidentity, e.g., at least 85%, at least 86%, at least 87%, at least 88%,at least 89%, at least 90%, at least 91%, at least 92%, at least 93%, atleast 94%, at least 95%, at least 96%, at least 97%, at least 98% or atleast 99% to the polypeptide of SEQ ID NO: 78. In one embodiment, thepolypeptides differ by up to 25 amino acids, e.g., between 1 and 25amino acids, such as 1-25, 1-20, 1-15, 1-10 or 1-5 amino acids, or 1, 2,3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, 15, 16, 17, 18, 19, 20, 21, 22,23, 24 or 25 amino acids from SEQ ID NO: 78. In one embodiment, thepolypeptide comprises or consists of the amino acid sequence of SEQ IDNO: 78; or is a fragment thereof having xylanase activity and having atleast 90% such as at least 91%, at least 92%, at least 93%, at least94%, at least 95%, at least 96%, at least 97%, at least 98% or at least99% of the length of the polypeptide. In another embodiment, polypeptidecomprises or consists of amino acids 1 to 181 of SEQ ID NO: 78.

The twenty-ninth aspect of the invention also relates to a method ofimproving one or more performance parameters of an animal comprisingadministering to one or more animals an animal feed additive comprisinga polypeptide having xylanase activity and having at least 80% sequenceidentity, e.g., at least 85%, at least 86%, at least 87%, at least 88%,at least 89%, at least 90%, at least 91%, at least 92%, at least 93%, atleast 94%, at least 95%, at least 96%, at least 97%, at least 98% or atleast 99% to the polypeptide of SEQ ID NO: 177. In one embodiment, thepolypeptides differ by up to 25 amino acids, e.g., between 1 and 25amino acids, such as 1-25, 1-20, 1-15, 1-10 or 1-5 amino acids, or 1, 2,3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, 15, 16, 17, 18, 19, 20, 21, 22,23, 24 or 25 amino acids from SEQ ID NO: 177. In one embodiment, thepolypeptide comprises or consists of the amino acid sequence of SEQ IDNO: 177; or is a fragment thereof having xylanase activity and having atleast 90% such as at least 91%, at least 92%, at least 93%, at least94%, at least 95%, at least 96%, at least 97%, at least 98% or at least99% of the length of the polypeptide. In another embodiment, polypeptidecomprises or consists of amino acids 1 to 323 of SEQ ID NO: 177.

In an embodiment, the plant based material from the sub-familyPanicoideae is maize, corn, sorghum, switchgrass, millet, pearl millet,foxtail millet or in a processed form such as milled corn, milled maize,defatted maize, defatted destarched maize, milled sorghum, milledswitchgrass, milled millet, milled foxtail millet, milled pearl millet,or any combination thereof. In a further embodiment, the plant basedmaterial from the sub-family Panicoideae is from the seed fraction (suchas endosperm and/or husk) of the plant.

Methods of Solubilising Xylose

In a thirtieth aspect, the invention relates to a method of solubilisingxylose from plant based material, comprising treating plant basedmaterial from the sub-family Panicoideae with the composition of thefirst aspect of the invention or any embodiment of the first aspect ofthe invention herein defined, such as in the section related to ‘GH62Polypeptides of the Composition’, or the section related to ‘GH10 andGH11 Polypeptides of the Composition’ or the section on ‘Combinations’or as described in any of the second to the twenty-eighth aspect of theinvention. In an embodiment, the plant based material from thesub-family Panicoideae is maize, corn, sorghum, switchgrass, millet,pearl millet, foxtail millet or in a processed form such as milled corn,milled maize, defatted maize, defatted destarched maize, milled sorghum,milled switchgrass, milled millet, milled foxtail millet, milled pearlmillet, or any combination thereof. In a further embodiment, the plantbased material from the sub-family Panicoideae is from the seed fraction(such as endosperm and/or husk) of the plant.

The thirtieth aspect of the invention also relates to a method ofsolubilising xylose from plant based material, comprising treating plantbased material from the sub-family Panicoideae with the composition ofthe first aspect of the invention or any embodiment herein defined (suchas in the section related to ‘GH62 Polypeptides of the Composition’, orthe section related to ‘GH10 and GH11 Polypeptides of the Composition’or the section on ‘Combinations’ or as described in any of the second tothe twenty-eighth aspect of the invention) and one or more formulatingagents. In a further embodiment, the plant based material from thesub-family Panicoideae is maize, corn, sorghum, switchgrass, millet,pearl millet, foxtail millet or in a processed form such as milled corn,milled maize, defatted maize, defatted destarched maize, milled sorghum,milled switchgrass, milled millet, milled foxtail millet, milled pearlmillet, or any combination thereof. In a further embodiment, the plantbased material from the sub-family Panicoideae is from the seed fraction(such as endosperm and/or husk) of the plant.

The thirtieth aspect of the invention further relates to a method ofsolubilising xylose from plant based material, comprising treating plantbased material from the sub-family Panicoideae with an animal feedadditive of the first aspect of the invention or any embodiment hereindefined (such as in the section related to ‘GH62 Polypeptides of theComposition’, or the section related to ‘GH10 and GH11 Polypeptides ofthe Composition’ or the section on ‘Combinations’ or as described in anyof the second to the twenty-eighth aspect of the invention) and one ormore formulating agents. In a further embodiment, the plant basedmaterial from the sub-family Panicoideae is maize, corn, sorghum,switchgrass, millet, pearl millet, foxtail millet or in a processed formsuch as milled corn, milled maize, defatted maize, defatted destarchedmaize, milled sorghum, milled switchgrass, milled millet, milled foxtailmillet, milled pearl millet, or any combination thereof. In a furtherembodiment, the plant based material from the sub-family Panicoideae isfrom the seed fraction (such as endosperm and/or husk) of the plant.

The thirtieth aspect of the invention further relates to a method ofsolubilising xylose from plant based material, comprising treating plantbased material from the sub-family Panicoideae with an animal feedadditive comprising a polypeptide having xylanase activity and having atleast 80% sequence identity, e.g., at least 85%, at least 86%, at least87%, at least 88%, at least 89%, at least 90%, at least 91%, at least92%, at least 93%, at least 94%, at least 95%, at least 96%, at least97%, at least 98% or at least 99% to the polypeptide of SEQ ID NO: 71.In one embodiment, the polypeptides differ by up to 25 amino acids,e.g., between 1 and 25 amino acids, such as 1-25, 1-20, 1-15, 1-10 or1-5 amino acids, or 1, 2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, 15,16, 17, 18, 19, 20, 21, 22, 23, 24 or 25 amino acids from SEQ ID NO: 71.In one embodiment, the polypeptide comprises or consists of the aminoacid sequence of SEQ ID NO: 71; or is a fragment thereof having xylanaseactivity and having at least 90% such as at least 91%, at least 92%, atleast 93%, at least 94%, at least 95%, at least 96%, at least 97%, atleast 98% or at least 99% of the length of the polypeptide. In anotherembodiment, polypeptide comprises or consists of amino acids 1 to 288 ofSEQ ID NO: 71.

The thirtieth aspect of the invention further relates to a method ofsolubilising xylose from plant based material, comprising treating plantbased material from the sub-family Panicoideae with an animal feedadditive comprising a polypeptide having xylanase activity and having atleast 80% sequence identity, e.g., at least 85%, at least 86%, at least87%, at least 88%, at least 89%, at least 90%, at least 91%, at least92%, at least 93%, at least 94%, at least 95%, at least 96%, at least97%, at least 98% or at least 99% to the polypeptide of SEQ ID NO: 78.In one embodiment, the polypeptides differ by up to 25 amino acids,e.g., between 1 and 25 amino acids, such as 1-25, 1-20, 1-15, 1-10 or1-5 amino acids, or 1, 2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, 15,16, 17, 18, 19, 20, 21, 22, 23, 24 or 25 amino acids from SEQ ID NO: 78.In one embodiment, the polypeptide comprises or consists of the aminoacid sequence of SEQ ID NO: 78; or is a fragment thereof having xylanaseactivity and having at least 90% such as at least 91%, at least 92%, atleast 93%, at least 94%, at least 95%, at least 96%, at least 97%, atleast 98% or at least 99% of the length of the polypeptide. In anotherembodiment, polypeptide comprises or consists of amino acids 1 to 181 ofSEQ ID NO: 78.

The thirtieth aspect of the invention further relates to a method ofsolubilising xylose from plant based material, comprising treating plantbased material from the sub-family Panicoideae with an animal feedadditive comprising a polypeptide having xylanase activity and having atleast 80% sequence identity, e.g., at least 85%, at least 86%, at least87%, at least 88%, at least 89%, at least 90%, at least 91%, at least92%, at least 93%, at least 94%, at least 95%, at least 96%, at least97%, at least 98% or at least 99% to the polypeptide of SEQ ID NO: 177.In one embodiment, the polypeptides differ by up to 25 amino acids,e.g., between 1 and 25 amino acids, such as 1-25, 1-20, 1-15, 1-10 or1-5 amino acids, or 1, 2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, 15,16, 17, 18, 19, 20, 21, 22, 23, 24 or 25 amino acids from SEQ ID NO:177. In one embodiment, the polypeptide comprises or consists of theamino acid sequence of SEQ ID NO: 177; or is a fragment thereof havingxylanase activity and having at least 90% such as at least 91%, at least92%, at least 93%, at least 94%, at least 95%, at least 96%, at least97%, at least 98% or at least 99% of the length of the polypeptide. Inanother embodiment, polypeptide comprises or consists of amino acids 1to 323 of SEQ ID NO: 177.

Methods of Releasing Starch

In a thirty-first aspect, the invention relates to a method of releasingstarch from plant based material, comprising treating plant basedmaterial from the sub-family Panicoideae with the composition of thefirst aspect of the invention or any embodiment of the first aspect ofthe invention herein defined, such as in the section related to ‘GH62Polypeptides of the Composition’, or the section related to ‘GH10 andGH11 Polypeptides of the Composition’ or the section on ‘Combinations’or as described in any of the second to the twenty-eighth aspect of theinvention. In an embodiment, the plant based material from thesub-family Panicoideae is maize, corn, sorghum, switchgrass, millet,pearl millet, foxtail millet or in a processed form such as milled corn,milled maize, defatted maize, defatted destarched maize, milled sorghum,milled switchgrass, milled millet, milled foxtail millet, milled pearlmillet, or any combination thereof. In a further embodiment, the plantbased material from the sub-family Panicoideae is from the seed fraction(such as endosperm and/or husk) of the plant.

The thirty-first aspect of the invention also relates to a method ofreleasing starch from plant based material, comprising treating plantbased material from the sub-family Panicoideae with the composition ofthe first aspect of the invention or any embodiment herein defined (suchas in the section related to ‘GH62 Polypeptides of the Composition’, orthe section related to ‘GH10 and GH11 Polypeptides of the Composition’or the section on ‘Combinations’ or as described in any of the second tothe twenty-eighth aspect of the invention) and one or more formulatingagents. In a further embodiment, the plant based material from thesub-family Panicoideae is maize, corn, sorghum, switchgrass, millet,pearl millet, foxtail millet or in a processed form such as milled corn,milled maize, defatted maize, defatted destarched maize, milled sorghum,milled switchgrass, milled millet, milled foxtail millet, milled pearlmillet, or any combination thereof. In a further embodiment, the plantbased material from the sub-family Panicoideae is from the seed fraction(such as endosperm and/or husk) of the plant.

The thirty-first aspect of the invention further relates to a method ofreleasing starch from plant based material, comprising treating plantbased material from the sub-family Panicoideae with an animal feedadditive of the first aspect of the invention or any embodiment hereindefined (such as in the section related to ‘GH62 Polypeptides of theComposition’, or the section related to ‘GH10 and GH11 Polypeptides ofthe Composition’ or the section on ‘Combinations’ or as described in anyof the second to the twenty-eighth aspect of the invention) and one ormore formulating agents. In a further embodiment, the plant basedmaterial from the sub-family Panicoideae is maize, corn, sorghum,switchgrass, millet, pearl millet, foxtail millet or in a processed formsuch as milled corn, milled maize, defatted maize, defatted destarchedmaize, milled sorghum, milled switchgrass, milled millet, milled foxtailmillet, milled pearl millet, or any combination thereof. In a furtherembodiment, the plant based material from the sub-family Panicoideae isfrom the seed fraction (such as endosperm and/or husk) of the plant.

Methods for Improving the Nutritional Value of an Animal Feed

The term improving the nutritional value of an animal feed meansimproving the availability of nutrients in the feed. In this inventionimproving the nutritional values refers in particular to improving thesolubilisation and degradation of the arabinoxylan-containing fraction(e.g. such as hemicellulose) of the feed, thereby leading to increasedrelease of nutrients from cells in the endosperm that have cell wallscomposed of highly recalcitrant hemicellulose. Consequently, an improvedarabinose and/or xylose extraction indicates a disruption of the cellwalls and as a result the nutritional value of the feed is improvedresulting in increased growth rate and/or weight gain and/or feedconversion (i.e. the weight of ingested feed relative to weight gain).In addition the arabinose and/or xylose release may result in improvedutilization of these components per se either directly or by bacterialfermentation in the hind gut thereby resulting in a production of shortchain fatty acids that may be readily absorbed in the hind and utilisedin the energy metabolism.

In a thirty-second aspect, the invention relates to a method forimproving the nutritional value of an animal feed comprising treatingthe animal feed comprising plant based material from the sub-familyPanicoideae with the composition of the first aspect of the invention orany embodiment of the first aspect of the invention herein defined, suchas in the section related to ‘GH62 Polypeptides of the Composition’, orthe section related to ‘GH10 and GH11 Polypeptides of the Composition’or the section on ‘Combinations’ or as described in any of the second tothe twenty-eighth aspect of the invention. In an embodiment, the plantbased material from the sub-family Panicoideae is maize, corn, sorghum,switchgrass, millet, pearl millet, foxtail millet or in a processed formsuch as milled corn, milled maize, defatted maize, defatted destarchedmaize, milled sorghum, milled switchgrass, milled millet, milled foxtailmillet, milled pearl millet, or any combination thereof. In a furtherembodiment, the plant based material from the sub-family Panicoideae isfrom the seed fraction (such as endosperm and/or husk) of the plant.

The thirty-second aspect of the invention also relates to a method forimproving the nutritional value of an animal feed comprising treatingthe animal feed comprising plant based material from the sub-familyPanicoideae with a polypeptide having xylanase activity and having atleast 80% sequence identity, e.g., at least 85%, at least 86%, at least87%, at least 88%, at least 89%, at least 90%, at least 91%, at least92%, at least 93%, at least 94%, at least 95%, at least 96%, at least97%, at least 98% or at least 99% to the polypeptide of SEQ ID NO: 71.In one embodiment, the polypeptides differ by up to 25 amino acids,e.g., between 1 and 25 amino acids, such as 1-25, 1-20, 1-15, 1-10 or1-5 amino acids, or 1, 2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, 15,16, 17, 18, 19, 20, 21, 22, 23, 24 or 25 amino acids from SEQ ID NO: 71.In one embodiment, the polypeptide comprises or consists of the aminoacid sequence of SEQ ID NO: 71; or is a fragment thereof having xylanaseactivity and having at least 90% such as at least 91%, at least 92%, atleast 93%, at least 94%, at least 95%, at least 96%, at least 97%, atleast 98% or at least 99% of the length of the polypeptide. In anotherembodiment, polypeptide comprises or consists of amino acids 1 to 288 ofSEQ ID NO: 71.

The thirty-second aspect of the invention also relates to a method forimproving the nutritional value of an animal feed comprising treatingthe animal feed comprising plant based material from the sub-familyPanicoideae with a polypeptide having xylanase activity and having atleast 80% sequence identity, e.g., at least 85%, at least 86%, at least87%, at least 88%, at least 89%, at least 90%, at least 91%, at least92%, at least 93%, at least 94%, at least 95%, at least 96%, at least97%, at least 98% or at least 99% to the polypeptide of SEQ ID NO: 78.In one embodiment, the polypeptides differ by up to 25 amino acids,e.g., between 1 and 25 amino acids, such as 1-25, 1-20, 1-15, 1-10 or1-5 amino acids, or 1, 2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, 15,16, 17, 18, 19, 20, 21, 22, 23, 24 or 25 amino acids from SEQ ID NO: 78.In one embodiment, the polypeptide comprises or consists of the aminoacid sequence of SEQ ID NO: 78; or is a fragment thereof having xylanaseactivity and having at least 90% such as at least 91%, at least 92%, atleast 93%, at least 94%, at least 95%, at least 96%, at least 97%, atleast 98% or at least 99% of the length of the polypeptide. In anotherembodiment, polypeptide comprises or consists of amino acids 1 to 181 ofSEQ ID NO: 78.

The thirty-second aspect of the invention also relates to a method forimproving the nutritional value of an animal feed comprising treatingthe animal feed comprising plant based material from the sub-familyPanicoideae with a polypeptide having xylanase activity and having atleast 80% sequence identity, e.g., at least 85%, at least 86%, at least87%, at least 88%, at least 89%, at least 90%, at least 91%, at least92%, at least 93%, at least 94%, at least 95%, at least 96%, at least97%, at least 98% or at least 99% to the polypeptide of SEQ ID NO: 177.In one embodiment, the polypeptides differ by up to 25 amino acids,e.g., between 1 and 25 amino acids, such as 1-25, 1-20, 1-15, 1-10 or1-5 amino acids, or 1, 2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, 15,16, 17, 18, 19, 20, 21, 22, 23, 24 or 25 amino acids from SEQ ID NO:177. In one embodiment, the polypeptide comprises or consists of theamino acid sequence of SEQ ID NO: 177; or is a fragment thereof havingxylanase activity and having at least 90% such as at least 91%, at least92%, at least 93%, at least 94%, at least 95%, at least 96%, at least97%, at least 98% or at least 99% of the length of the polypeptide. Inanother embodiment, polypeptide comprises or consists of amino acids 1to 323 of SEQ ID NO: 177.

Methods of Preparing an Animal Feed

In a thirty-third aspect, the invention relates to a method of preparingan animal feed, comprising mixing the composition of the first aspect ofthe invention or any embodiment herein defined (such as in the sectionrelated to ‘GH62 Polypeptides of the Composition’, or the sectionrelated to ‘GH10 and GH11 Polypeptides of the Composition’ or thesection on ‘Combinations’ or as described in any of the second to thetwenty-eighth aspect of the invention) with plant based material fromthe sub-family Panicoideae, such as maize, corn, sorghum, switchgrass,millet, pearl millet, foxtail millet or in a processed form such asmilled corn, milled maize, defatted maize, defatted destarched maize,milled sorghum, milled switchgrass, milled millet, milled foxtailmillet, milled pearl millet, or any combination thereof. In a preferredembodiment, the plant based material from the sub-family Panicoideae isfrom the seed fraction (such as endosperm and/or husk) of the plant,preferable the seed fraction from maize, corn, sorghum, switchgrass,millet, pearl millet, foxtail millet or the processed from thereof, suchas milled corn, milled maize, defatted maize, defatted destarched maize,milled sorghum, milled switchgrass, milled millet, milled foxtailmillet, milled pearl millet, or any combination thereof. In anotherpreferred embodiment, the plant based material from the sub-familyPanicoideae is from a plant part comprising highly branched xylan, suchas the seed fraction (such as endosperm and/or husk) of the plant.

Polynucleotides

The present invention also relates to isolated polynucleotides encodinga polypeptide of the present invention.

The techniques used to isolate or clone a polynucleotide are known inthe art and include isolation from genomic DNA or cDNA, or a combinationthereof. The cloning of the polynucleotides from genomic DNA can beeffected, e.g., by using the well-known polymerase chain reaction (PCR)or antibody screening of expression libraries to detect cloned DNAfragments with shared structural features. See, e.g., Innis et al.,1990, PCR: A Guide to Methods and Application, Academic Press, New York.Other nucleic acid amplification procedures such as ligase chainreaction (LCR), ligation activated transcription (LAT) andpolynucleotide-based amplification (NASBA) may be used. Thepolynucleotides may be cloned from a strain of Bacillus, or a relatedorganism and thus, for example, may be an allelic or species variant ofthe polypeptide encoding region of the polynucleotide.

The present invention also relates to isolated polynucleotidescomprising or consisting of polynucleotides having a degree of sequenceidentity to the mature polypeptide coding sequence of SEQ ID NO: 10 ofat least of at least 85%, e.g., at least 86%, at least 87%, at least88%, at least 89%, at least 90%, at least 91%, at least 92%, at least93%, at least 94%, at least 95%, at least 96%, at least 97%, at least98%, at least 99%, or 100%, which encode a polypeptide havingarabinofuranosidase activity.

The present invention also relates to isolated polynucleotidescomprising or consisting of polynucleotides having a degree of sequenceidentity to the mature polypeptide coding sequence of SEQ ID NO: 25 ofat least of at least 80%, e.g., at least 85%, at least 86%, at least87%, at least 88%, at least 89%, at least 90%, at least 91%, at least92%, at least 93%, at least 94%, at least 95%, at least 96%, at least97%, at least 98%, at least 99%, or 100% which encode a polypeptidehaving arabinofuranosidase activity.

The present invention also relates to isolated polynucleotidescomprising or consisting of polynucleotides having a degree of sequenceidentity to the mature polypeptide coding sequence of SEQ ID NO: 28 ofat least of at least 90%, e.g., at least 91%, at least 92%, at least93%, at least 94%, at least 95%, at least 96%, at least 97%, at least98%, at least 99%, or 100% which encode a polypeptide havingarabinofuranosidase activity.

The present invention also relates to isolated polynucleotidescomprising or consisting of polynucleotides having a degree of sequenceidentity to the mature polypeptide coding sequence of SEQ ID NO: 34 ofat least of at least 92%, e.g., at least 93%, at least 94%, at least95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100%which encode a polypeptide having arabinofuranosidase activity.

The present invention also relates to isolated polynucleotidescomprising or consisting of polynucleotides having a degree of sequenceidentity to the mature polypeptide coding sequence of SEQ ID NO: 46 ofat least of at least 86%, e.g., at least 87%, at least 88%, at least89%, at least 90%, at least 91%, at least 92%, at least 93%, at least94%, at least 95%, at least 96%, at least 97%, at least 98%, at least99%, or 100% which encode a polypeptide having arabinofuranosidaseactivity.

The present invention also relates to isolated polynucleotidescomprising or consisting of polynucleotides having a degree of sequenceidentity to the mature polypeptide coding sequence of SEQ ID NO: 52 ofat least of at least 80%, e.g., at least 85%, at least 86%, at least87%, at least 88%, at least 89%, at least 90%, at least 91%, at least92%, at least 93%, at least 94%, at least 95%, at least 96%, at least97%, at least 98%, at least 99%, or 100% which encode a polypeptidehaving arabinofuranosidase activity.

The present invention also relates to isolated polynucleotidescomprising or consisting of polynucleotides having a degree of sequenceidentity to the mature polypeptide coding sequence of SEQ ID NO: 58 ofat least of at least 81%, e.g., at least 85%, at least 86%, at least87%, at least 88%, at least 89%, at least 90%, at least 91%, at least92%, at least 93%, at least 94%, at least 95%, at least 96%, at least97%, at least 98%, at least 99%, or 100% which encode a polypeptidehaving arabinofuranosidase activity.

The present invention also relates to isolated polynucleotidescomprising or consisting of polynucleotides having a degree of sequenceidentity to the mature polypeptide coding sequence of SEQ ID NO: 64 ofat least of at least 81%, e.g., at least 85%, at least 86%, at least87%, at least 88%, at least 89%, at least 90%, at least 91%, at least92%, at least 93%, at least 94%, at least 95%, at least 96%, at least97%, at least 98%, at least 99%, or 100% which encode a polypeptidehaving arabinofuranosidase activity.

The present invention also relates to isolated polynucleotidescomprising or consisting of polynucleotides having a degree of sequenceidentity to the mature polypeptide coding sequence of SEQ ID NO: 82 ofat least of at least 84%, e.g., at least 85%, at least 86%, at least87%, at least 88%, at least 89%, at least 90%, at least 91%, at least92%, at least 93%, at least 94%, at least 95%, at least 96%, at least97%, at least 98%, at least 99%, or 100% which encode a polypeptidehaving xylanase activity.

The present invention also relates to isolated polynucleotidescomprising or consisting of polynucleotides having a degree of sequenceidentity to the mature polypeptide coding sequence of SEQ ID NO: 97 ofat least of at least 80%, e.g., at least 85%, at least 86%, at least87%, at least 88%, at least 89%, at least 90%, at least 91%, at least92%, at least 93%, at least 94%, at least 95%, at least 96%, at least97%, at least 98%, at least 99%, or 100% which encode a polypeptidehaving xylanase activity.

The present invention also relates to isolated polynucleotidescomprising or consisting of polynucleotides having a degree of sequenceidentity to the mature polypeptide coding sequence of SEQ ID NO: 100 ofat least of at least 80%, e.g., at least 85%, at least 86%, at least87%, at least 88%, at least 89%, at least 90%, at least 91%, at least92%, at least 93%, at least 94%, at least 95%, at least 96%, at least97%, at least 98%, at least 99%, or 100% which encode a polypeptidehaving xylanase activity.

The present invention also relates to isolated polynucleotidescomprising or consisting of polynucleotides having a degree of sequenceidentity to the mature polypeptide coding sequence of SEQ ID NO: 103 ofat least of at least 87%, e.g., at least 88%, at least 89%, at least90%, at least 91%, at least 92%, at least 93%, at least 94%, at least95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100%which encode a polypeptide having arabinofuranosidase activity.

The present invention also relates to isolated polynucleotidescomprising or consisting of polynucleotides having a degree of sequenceidentity to the mature polypeptide coding sequence of SEQ ID NO: 106 ofat least of at least 85%, e.g., at least 86%, at least 87%, at least88%, at least 89%, at least 90%, at least 91%, at least 92%, at least93%, at least 94%, at least 95%, at least 96%, at least 97%, at least98%, at least 99%, or 100% which encode a polypeptide havingarabinofuranosidase activity.

The present invention also relates to isolated polynucleotidescomprising or consisting of polynucleotides having a degree of sequenceidentity to the mature polypeptide coding sequence of SEQ ID NO: 112 ofat least of at least 80%, e.g., at least 85%, at least 86%, at least87%, at least 88%, at least 89%, at least 90%, at least 91%, at least92%, at least 93%, at least 94%, at least 95%, at least 96%, at least97%, at least 98%, at least 99%, or 100% which encode a polypeptidehaving arabinofuranosidase activity.

The present invention also relates to isolated polynucleotidescomprising or consisting of polynucleotides having a degree of sequenceidentity to the mature polypeptide coding sequence of SEQ ID NO: 118 ofat least of at least 80%, e.g., at least 85%, at least 86%, at least87%, at least 88%, at least 89%, at least 90%, at least 91%, at least92%, at least 93%, at least 94%, at least 95%, at least 96%, at least97%, at least 98%, at least 99%, or 100% which encode a polypeptidehaving arabinofuranosidase activity.

The present invention also relates to isolated polynucleotidescomprising or consisting of polynucleotides having a degree of sequenceidentity to the mature polypeptide coding sequence of SEQ ID NO: 121 ofat least of at least 89%, e.g., at least 90%, at least 91%, at least92%, at least 93%, at least 94%, at least 95%, at least 96%, at least97%, at least 98%, at least 99%, or 100% which encode a polypeptidehaving arabinofuranosidase activity.

The present invention also relates to isolated polynucleotidescomprising or consisting of polynucleotides having a degree of sequenceidentity to the mature polypeptide coding sequence of SEQ ID NO: 124 ofat least of at least 80%, e.g., at least 85%, at least 86%, at least87%, at least 88%, at least 89%, at least 90%, at least 91%, at least92%, at least 93%, at least 94%, at least 95%, at least 96%, at least97%, at least 98%, at least 99%, or 100% which encode a polypeptidehaving arabinofuranosidase activity.

The present invention also relates to isolated polynucleotidescomprising or consisting of polynucleotides having a degree of sequenceidentity to the mature polypeptide coding sequence of SEQ ID NO: 136 ofat least of at least 84%, e.g., at least 85%, at least 86%, at least87%, at least 88%, at least 89%, at least 90%, at least 91%, at least92%, at least 93%, at least 94%, at least 95%, at least 96%, at least97%, at least 98%, at least 99%, or 100% which encode a polypeptidehaving arabinofuranosidase activity.

The present invention also relates to isolated polynucleotidescomprising or consisting of polynucleotides having a degree of sequenceidentity to the mature polypeptide coding sequence of SEQ ID NO: 139 ofat least of at least 89%, e.g., at least 90%, at least 91%, at least92%, at least 93%, at least 94%, at least 95%, at least 96%, at least97%, at least 98%, at least 99%, or 100% which encode a polypeptidehaving arabinofuranosidase activity.

The present invention also relates to isolated polynucleotidescomprising or consisting of polynucleotides having a degree of sequenceidentity to the mature polypeptide coding sequence of SEQ ID NO: 145 ofat least of at least 86%, e.g., at least 87%, at least 88%, at least89%, at least 90%, at least 91%, at least 92%, at least 93%, at least94%, at least 95%, at least 96%, at least 97%, at least 98%, at least99%, or 100% which encode a polypeptide having arabinofuranosidaseactivity.

The present invention also relates to isolated polynucleotidescomprising or consisting of polynucleotides having a degree of sequenceidentity to the mature polypeptide coding sequence of SEQ ID NO: 154 ofat least of at least 97%, e.g., at least 98%, at least 99%, or 100%which encode a polypeptide having arabinofuranosidase activity.

The present invention also relates to isolated polynucleotidescomprising or consisting of polynucleotides having a degree of sequenceidentity to the mature polypeptide coding sequence of SEQ ID NO: 157 ofat least of at least 97%, e.g., at least 98%, at least 99%, or 100%which encode a polypeptide having arabinofuranosidase activity.

The present invention also relates to isolated polynucleotidescomprising or consisting of polynucleotides having a degree of sequenceidentity to the mature polypeptide coding sequence of SEQ ID NO: 160 ofat least of at least 80%, e.g., at least 85%, at least 86%, at least87%, at least 88%, at least 89%, at least 90%, at least 91%, at least92%, at least 93%, at least 94%, at least 95%, at least 96%, at least97%, at least 98%, at least 99%, or 100% which encode a polypeptidehaving arabinofuranosidase activity.

The present invention also relates to isolated polynucleotidescomprising or consisting of polynucleotides having a degree of sequenceidentity to the mature polypeptide coding sequence of SEQ ID NO: 163 ofat least of at least 80%, e.g., at least 85%, at least 86%, at least87%, at least 88%, at least 89%, at least 90%, at least 91%, at least92%, at least 93%, at least 94%, at least 95%, at least 96%, at least97%, at least 98%, at least 99%, or 100% which encode a polypeptidehaving arabinofuranosidase activity.

The present invention also relates to isolated polynucleotidescomprising or consisting of polynucleotides having a degree of sequenceidentity to the mature polypeptide coding sequence of SEQ ID NO: 166 ofat least of at least 80%, e.g., at least 85%, at least 86%, at least87%, at least 88%, at least 89%, at least 90%, at least 91%, at least92%, at least 93%, at least 94%, at least 95%, at least 96%, at least97%, at least 98%, at least 99%, or 100% which encode a polypeptidehaving arabinofuranosidase activity.

The present invention also relates to isolated polynucleotidescomprising or consisting of polynucleotides having a degree of sequenceidentity to the mature polypeptide coding sequence of SEQ ID NO: 169 ofat least of at least 80%, e.g., at least 85%, at least 86%, at least87%, at least 88%, at least 89%, at least 90%, at least 91%, at least92%, at least 93%, at least 94%, at least 95%, at least 96%, at least97%, at least 98%, at least 99%, or 100% which encode a polypeptidehaving arabinofuranosidase activity.

The present invention also relates to isolated polynucleotidescomprising or consisting of polynucleotides having a degree of sequenceidentity to the mature polypeptide coding sequence of SEQ ID NO: 172 ofat least of at least 80%, e.g., at least 85%, at least 86%, at least87%, at least 88%, at least 89%, at least 90%, at least 91%, at least92%, at least 93%, at least 94%, at least 95%, at least 96%, at least97%, at least 98%, at least 99%, or 100% which encode a polypeptidehaving arabinofuranosidase activity.

Modification of a polynucleotide encoding a polypeptide of the presentinvention may be necessary for synthesizing polypeptides substantiallysimilar to the polypeptide. The term “substantially similar” to thepolypeptide refers to non-naturally occurring forms of the polypeptide.

Nucleic Acid Constructs

The present invention also relates to nucleic acid constructs comprisinga polynucleotide of the present invention operably linked to one or morecontrol sequences that direct the expression of the coding sequence in asuitable host cell under conditions compatible with the controlsequences.

The polynucleotide may be manipulated in a variety of ways to providefor expression of the polypeptide. Manipulation of the polynucleotideprior to its insertion into a vector may be desirable or necessarydepending on the expression vector. The techniques for modifyingpolynucleotides utilizing recombinant DNA methods are well known in theart.

The control sequence may be a promoter, a polynucleotide that isrecognized by a host cell for expression of a polynucleotide encoding apolypeptide of the present invention. The promoter containstranscriptional control sequences that mediate the expression of thepolypeptide. The promoter may be any polynucleotide that showstranscriptional activity in the host cell including mutant, truncated,and hybrid promoters, and may be obtained from genes encodingextracellular or intracellular polypeptides either homologous orheterologous to the host cell.

Examples of suitable promoters for directing transcription of thenucleic acid constructs of the present invention in a bacterial hostcell are the promoters obtained from the Bacillus amyloliquefaciensalpha-amylase gene (amyQ), Bacillus licheniformis alpha-amylase gene(amyL), Bacillus licheniformis penicillinase gene (penP), Bacillusstearothermophilus maltogenic amylase gene (amyM), Bacillus subtilislevansucrase gene (sacB), Bacillus subtilis xylA and xylB genes,Bacillus thuringiensis cryllIA gene (Agaisse and Lereclus, 1994,Molecular Microbiology 13: 97-107), E. coli lac operon, E. coli trcpromoter (Egon et al., 1988, Gene 69: 301-315), Streptomyces coelicoloragarase gene (dagA), and prokaryotic beta-lactamase gene (Villa-Kamaroffet al., 1978, Proc. Natl. Acad. Sci. USA 75: 3727-3731), as well as thetac promoter (DeBoer et al., 1983, Proc. Natl. Acad. Sci. USA 80:21-25). Further promoters are described in “Useful proteins fromrecombinant bacteria” in Gilbert et al., 1980, Scientific American 242:74-94; and in Sambrook et al., 1989, supra. Examples of tandem promotersare disclosed in WO 99/43835.

Examples of suitable promoters for directing transcription of thenucleic acid constructs of the present invention in a filamentous fungalhost cell are promoters obtained from the genes for Aspergillus nidulansacetamidase, Aspergillus niger neutral alpha-amylase, Aspergillus nigeracid stable alpha-amylase, Aspergillus niger or Aspergillus awamoriglucoamylase (glaA), Aspergillus oryzae TAKA amylase, Aspergillus oryzaealkaline protease, Aspergillus oryzae triose phosphate isomerase,Fusarium oxysporum trypsin-like protease (WO 96/00787), Fusariumvenenatum amyloglucosidase (WO 00/56900), Fusarium venenatum Daria (WO00/56900), Fusarium venenatum Quinn (WO 00/56900), Rhizomucor mieheilipase, Rhizomucor miehei aspartic proteinase, Trichoderma reeseibeta-glucosidase, Trichoderma reesei cellobiohydrolase I, Trichodermareesei cellobiohydrolase II, Trichoderma reesei endoglucanase I,Trichoderma reesei endoglucanase II, Trichoderma reesei endoglucanaseIII, Trichoderma reesei endoglucanase V, Trichoderma reesei xylanase I,Trichoderma reesei xylanase II, Trichoderma reesei xylanase III,Trichoderma reesei beta-xylosidase, and Trichoderma reesei translationelongation factor, as well as the NA2-tpi promoter (a modified promoterfrom an Aspergillus neutral alpha-amylase gene in which the untranslatedleader has been replaced by an untranslated leader from an Aspergillustriose phosphate isomerase gene; non-limiting examples include modifiedpromoters from an Aspergillus niger neutral alpha-amylase gene in whichthe untranslated leader has been replaced by an untranslated leader froman Aspergillus nidulans or Aspergillus oryzae triose phosphate isomerasegene); and mutant, truncated, and hybrid promoters thereof. Otherpromoters are described in U.S. Pat. No. 6,011,147.

In a yeast host, useful promoters are obtained from the genes forSaccharomyces cerevisiae enolase (ENO-1), Saccharomyces cerevisiaegalactokinase (GAL1), Saccharomyces cerevisiae alcoholdehydrogenase/glyceraldehyde-3-phosphate dehydrogenase (ADH1, ADH2/GAP),Saccharomyces cerevisiae triose phosphate isomerase (TPI), Saccharomycescerevisiae metallothionein (CUP1), and Saccharomyces cerevisiae3-phosphoglycerate kinase. Other useful promoters for yeast host cellsare described by Romanos et al., 1992, Yeast 8: 423-488.

The control sequence may also be a transcription terminator, which isrecognized by a host cell to terminate transcription. The terminator isoperably linked to the 3′-terminus of the polynucleotide encoding thepolypeptide. Any terminator that is functional in the host cell may beused in the present invention.

Preferred terminators for bacterial host cells are obtained from thegenes for Bacillus clausii alkaline protease (aprH), Bacilluslicheniformis alpha-amylase (amyL), and Escherichia coli ribosomal RNA(rrnB).

Preferred terminators for filamentous fungal host cells are obtainedfrom the genes for Aspergillus nidulans acetamidase, Aspergillusnidulans anthranilate synthase, Aspergillus niger glucoamylase,Aspergillus niger alpha-glucosidase, Aspergillus oryzae TAKA amylase,Fusarium oxysporum trypsin-like protease, Trichoderma reeseibeta-glucosidase, Trichoderma reesei cellobiohydrolase I, Trichodermareesei cellobiohydrolase II, Trichoderma reesei endoglucanase I,Trichoderma reesei endoglucanase II, Trichoderma reesei endoglucanaseIII, Trichoderma reesei endoglucanase V, Trichoderma reesei xylanase I,Trichoderma reesei xylanase II, Trichoderma reesei xylanase III,Trichoderma reesei beta-xylosidase, and Trichoderma reesei translationelongation factor.

Preferred terminators for yeast host cells are obtained from the genesfor Saccharomyces cerevisiae enolase, Saccharomyces cerevisiaecytochrome C (CYC1), and Saccharomyces cerevisiaeglyceraldehyde-3-phosphate dehydrogenase. Other useful terminators foryeast host cells are described by Romanos et al., 1992, supra.

The control sequence may also be an mRNA stabilizer region downstream ofa promoter and upstream of the coding sequence of a gene which increasesexpression of the gene.

Examples of suitable mRNA stabilizer regions are obtained from aBacillus thuringiensis cryllIA gene (WO 94/25612) and a Bacillussubtilis SP82 gene (Hue et al., 1995, Journal of Bacteriology 177:3465-3471).

The control sequence may also be a leader, a nontranslated region of anmRNA that is important for translation by the host cell. The leader isoperably linked to the 5′-terminus of the polynucleotide encoding thepolypeptide. Any leader that is functional in the host cell may be used.

Preferred leaders for filamentous fungal host cells are obtained fromthe genes for Aspergillus oryzae TAKA amylase and Aspergillus nidulanstriose phosphate isomerase.

Suitable leaders for yeast host cells are obtained from the genes forSaccharomyces cerevisiae enolase (ENO-1), Saccharomyces cerevisiae3-phosphoglycerate kinase, Saccharomyces cerevisiae alpha-factor, andSaccharomyces cerevisiae alcoholdehydrogenase/glyceraldehyde-3-phosphate dehydrogenase (ADH2/GAP).

The control sequence may also be a polyadenylation sequence, a sequenceoperably linked to the 3′-terminus of the polynucleotide and, whentranscribed, is recognized by the host cell as a signal to addpolyadenosine residues to transcribed mRNA. Any polyadenylation sequencethat is functional in the host cell may be used.

Preferred polyadenylation sequences for filamentous fungal host cellsare obtained from the genes for Aspergillus nidulans anthranilatesynthase, Aspergillus niger glucoamylase, Aspergillus nigeralpha-glucosidase Aspergillus oryzae TAKA amylase, and Fusariumoxysporum trypsin-like protease.

Useful polyadenylation sequences for yeast host cells are described byGuo and Sherman, 1995, Mol. Cellular Biol. 15: 5983-5990.

The control sequence may also be a signal peptide coding region thatencodes a signal peptide linked to the N-terminus of a polypeptide anddirects the polypeptide into the cell's secretory pathway. The 5′-end ofthe coding sequence of the polynucleotide may inherently contain asignal peptide coding sequence naturally linked in translation readingframe with the segment of the coding sequence that encodes thepolypeptide. Alternatively, the 5′-end of the coding sequence maycontain a signal peptide coding sequence that is foreign to the codingsequence. A foreign signal peptide coding sequence may be required wherethe coding sequence does not naturally contain a signal peptide codingsequence. Alternatively, a foreign signal peptide coding sequence maysimply replace the natural signal peptide coding sequence in order toenhance secretion of the polypeptide. However, any signal peptide codingsequence that directs the expressed polypeptide into the secretorypathway of a host cell may be used.

Effective signal peptide coding sequences for bacterial host cells arethe signal peptide coding sequences obtained from the genes for BacillusNCIB 11837 maltogenic amylase, Bacillus licheniformis subtilisin,Bacillus licheniformis beta-lactamase, Bacillus stearothermophilusalpha-amylase, Bacillus stearothermophilus neutral proteases (nprT,nprS, nprM), and Bacillus subtilis prsA. Further signal peptides aredescribed by Simonen and Palva, 1993, Microbiological Reviews 57:109-137.

Effective signal peptide coding sequences for filamentous fungal hostcells are the signal peptide coding sequences obtained from the genesfor Aspergillus niger neutral amylase, Aspergillus niger glucoamylase,Aspergillus oryzae TAKA amylase, Humicola insolens cellulase, Humicolainsolens endoglucanase V, Humicola lanuginosa lipase, and Rhizomucormiehei aspartic proteinase.

Useful signal peptides for yeast host cells are obtained from the genesfor Saccharomyces cerevisiae alpha-factor and Saccharomyces cerevisiaeinvertase. Other useful signal peptide coding sequences are described byRomanos et al., 1992, supra.

The control sequence may also be a propeptide coding sequence thatencodes a propeptide positioned at the N-terminus of a polypeptide. Theresultant polypeptide is known as a proenzyme or propolypeptide (or azymogen in some cases). A propolypeptide is generally inactive and canbe converted to an active polypeptide by catalytic or autocatalyticcleavage of the propeptide from the propolypeptide. The propeptidecoding sequence may be obtained from the genes for Bacillus subtilisalkaline protease (aprE), Bacillus subtilis neutral protease (nprT),Myceliophthora thermophila laccase (WO 95/33836), Rhizomucor mieheiaspartic proteinase, and Saccharomyces cerevisiae alpha-factor.

Where both signal peptide and propeptide sequences are present, thepropeptide sequence is positioned next to the N-terminus of apolypeptide and the signal peptide sequence is positioned next to theN-terminus of the propeptide sequence.

It may also be desirable to add regulatory sequences that regulateexpression of the polypeptide relative to the growth of the host cell.Examples of regulatory sequences are those that cause expression of thegene to be turned on or off in response to a chemical or physicalstimulus, including the presence of a regulatory compound. Regulatorysequences in prokaryotic systems include the lac, tac, and trp operatorsystems. In yeast, the ADH2 system or GAL1 system may be used. Infilamentous fungi, the Aspergillus niger glucoamylase promoter,Aspergillus oryzae TAKA alpha-amylase promoter, and Aspergillus oryzaeglucoamylase promoter, Trichoderma reesei cellobiohydrolase I promoter,and Trichoderma reesei cellobiohydrolase II promoter may be used. Otherexamples of regulatory sequences are those that allow for geneamplification. In eukaryotic systems, these regulatory sequences includethe dihydrofolate reductase gene that is amplified in the presence ofmethotrexate, and the metallothionein genes that are amplified withheavy metals. In these cases, the polynucleotide encoding thepolypeptide would be operably linked to the regulatory sequence.

Expression Vectors

The present invention also relates to recombinant expression vectorscomprising a polynucleotide of the present invention, a promoter, andtranscriptional and translational stop signals. The various nucleotideand control sequences may be joined together to produce a recombinantexpression vector that may include one or more convenient restrictionsites to allow for insertion or substitution of the polynucleotideencoding the polypeptide at such sites. Alternatively, thepolynucleotide may be expressed by inserting the polynucleotide or anucleic acid construct comprising the polynucleotide into an appropriatevector for expression. In creating the expression vector, the codingsequence is located in the vector so that the coding sequence isoperably linked with the appropriate control sequences for expression.

The recombinant expression vector may be any vector (e.g., a plasmid orvirus) that can be conveniently subjected to recombinant DNA proceduresand can bring about expression of the polynucleotide. The choice of thevector will typically depend on the compatibility of the vector with thehost cell into which the vector is to be introduced. The vector may be alinear or closed circular plasmid.

The vector may be an autonomously replicating vector, i.e., a vectorthat exists as an extrachromosomal entity, the replication of which isindependent of chromosomal replication, e.g., a plasmid, anextrachromosomal element, a minichromosome, or an artificial chromosome.The vector may contain any means for assuring self-replication.Alternatively, the vector may be one that, when introduced into the hostcell, is integrated into the genome and replicated together with thechromosome(s) into which it has been integrated. Furthermore, a singlevector or plasmid or two or more vectors or plasmids that togethercontain the total DNA to be introduced into the genome of the host cell,or a transposon, may be used.

The vector preferably contains one or more selectable markers thatpermit easy selection of transformed, transfected, transduced, or thelike cells. A selectable marker is a gene the product of which providesfor biocide or viral resistance, resistance to heavy metals, prototrophyto auxotrophs, and the like.

Examples of bacterial selectable markers are Bacillus licheniformis orBacillus subtilis dal genes, or markers that confer antibioticresistance such as ampicillin, chloramphenicol, kanamycin, neomycin,spectinomycin, or tetracycline resistance. Suitable markers for yeasthost cells include, but are not limited to, ADE2, HIS3, LEU2, LYS2,METS, TRP1, and URA3. Selectable markers for use in a filamentous fungalhost cell include, but are not limited to, adeA(phosphoribosylaminoimidazole-succinocarboxamide synthase), adeB(phosphoribosyl-aminoimidazole synthase), amdS (acetamidase), argB(ornithine carbamoyltransferase), bar (phosphinothricinacetyltransferase), hph (hygromycin phosphotransferase), niaD (nitratereductase), pyrG (orotidine-5′-phosphate decarboxylase), sC (sulfateadenyltransferase), and trpC (anthranilate synthase), as well asequivalents thereof. Preferred for use in an Aspergillus cell areAspergillus nidulans or Aspergillus oryzae amdS and pyrG genes and aStreptomyces hygroscopicus bar gene. Preferred for use in a Trichodermacell are adeA, adeB, amdS, hph, and pyrG genes.

The selectable marker may be a dual selectable marker system asdescribed in WO 2010/039889. In one aspect, the dual selectable markeris an hph-tk dual selectable marker system.

The vector preferably contains an element(s) that permits integration ofthe vector into the host cell's genome or autonomous replication of thevector in the cell independent of the genome.

For integration into the host cell genome, the vector may rely on thepolynucleotide's sequence encoding the polypeptide or any other elementof the vector for integration into the genome by homologous ornon-homologous recombination. Alternatively, the vector may containadditional polynucleotides for directing integration by homologousrecombination into the genome of the host cell at a precise location(s)in the chromosome(s). To increase the likelihood of integration at aprecise location, the integrational elements should contain a sufficientnumber of nucleic acids, such as 100 to 10,000 base pairs, 400 to 10,000base pairs, and 800 to 10,000 base pairs, which have a high degree ofsequence identity to the corresponding target sequence to enhance theprobability of homologous recombination. The integrational elements maybe any sequence that is homologous with the target sequence in thegenome of the host cell. Furthermore, the integrational elements may benon-encoding or encoding polynucleotides. On the other hand, the vectormay be integrated into the genome of the host cell by non-homologousrecombination.

For autonomous replication, the vector may further comprise an origin ofreplication enabling the vector to replicate autonomously in the hostcell in question. The origin of replication may be any plasmidreplicator mediating autonomous replication that functions in a cell.The term “origin of replication” or “plasmid replicator” means apolynucleotide that enables a plasmid or vector to replicate in vivo.

Examples of bacterial origins of replication are the origins ofreplication of plasmids pBR322, pUC19, pACYC177, and pACYC184 permittingreplication in E. coli, and pUB110, pE194, pTA1060, and pAMβ1 permittingreplication in Bacillus.

Examples of origins of replication for use in a yeast host cell are the2 micron origin of replication, ARS1, ARS4, the combination of ARS1 andCEN3, and the combination of ARS4 and CEN6.

Examples of origins of replication useful in a filamentous fungal cellare AMA1 and ANS1 (Gems et al., 1991, Gene 98: 61-67; Cullen et al.,1987, Nucleic Acids Res. 15: 9163-9175; WO 00/24883). Isolation of theAMA1 gene and construction of plasmids or vectors comprising the genecan be accomplished according to the methods disclosed in WO 00/24883.

More than one copy of a polynucleotide of the present invention may beinserted into a host cell to increase production of a polypeptide. Anincrease in the copy number of the polynucleotide can be obtained byintegrating at least one additional copy of the sequence into the hostcell genome or by including an amplifiable selectable marker gene withthe polynucleotide where cells containing amplified copies of theselectable marker gene, and thereby additional copies of thepolynucleotide, can be selected for by cultivating the cells in thepresence of the appropriate selectable agent.

The procedures used to ligate the elements described above to constructthe recombinant expression vectors of the present invention are wellknown to one skilled in the art (see, e.g., Sambrook et al., 1989,supra).

Host Cells

The present invention also relates to recombinant host cells, comprisinga polynucleotide of the present invention operably linked to one or morecontrol sequences that direct the production of a polypeptide of thepresent invention. A construct or vector comprising a polynucleotide isintroduced into a host cell so that the construct or vector ismaintained as a chromosomal integrant or as a self-replicatingextra-chromosomal vector as described earlier. The term “host cell”encompasses any progeny of a parent cell that is not identical to theparent cell due to mutations that occur during replication. The choiceof a host cell will to a large extent depend upon the gene encoding thepolypeptide and its source.

The host cell may be any cell useful in the recombinant production of apolypeptide of the present invention, e.g., a prokaryote or a eukaryote.

The prokaryotic host cell may be any Gram-positive or Gram-negativebacterium. Gram-positive bacteria include, but are not limited to,Bacillus, Clostridium, Enterococcus, Geobacillus, Lactobacillus,Lactococcus, Oceanobacillus, Staphylococcus, Streptococcus, andStreptomyces. Gram-negative bacteria include, but are not limited to,Campylobacter, E. coli, Flavobacterium, Fusobacterium, Helicobacter,Ilyobacter, Neisseria, Pseudomonas, Salmonella, and Ureaplasma.

The bacterial host cell may be any Bacillus cell including, but notlimited to, Bacillus alkalophilus, Bacillus amyloliquefaciens, Bacillusbrevis, Bacillus circulans, Bacillus clausii, Bacillus coagulans,Bacillus firmus, Bacillus lautus, Bacillus lentus, Bacilluslicheniformis, Bacillus megaterium, Bacillus pumilus, Bacillusstearothermophilus, Bacillus subtilis, and Bacillus thuringiensis cells.

The bacterial host cell may also be any Streptococcus cell including,but not limited to, Streptococcus equisimilis, Streptococcus pyogenes,Streptococcus uberis, and Streptococcus equi subsp. Zooepidemicus cells.

The bacterial host cell may also be any Streptomyces cell including, butnot limited to, Streptomyces achromogenes, Streptomyces avermitilis,Streptomyces coelicolor, Streptomyces griseus, and Streptomyces lividanscells.

The introduction of DNA into a Bacillus cell may be effected byprotoplast transformation (see, e.g., Chang and Cohen, 1979, Mol. Gen.Genet. 168: 111-115), competent cell transformation (see, e.g., Youngand Spizizen, 1961, J. Bacteriol. 81: 823-829, or Dubnau andDavidoff-Abelson, 1971, J. Mol. Biol. 56: 209-221), electroporation(see, e.g., Shigekawa and Dower, 1988, Biotechniques 6: 742-751), orconjugation (see, e.g., Koehler and Thorne, 1987, J. Bacteriol. 169:5271-5278). The introduction of DNA into an E. coli cell may be effectedby protoplast transformation (see, e.g., Hanahan, 1983, J. Mol. Biol.166: 557-580) or electroporation (see, e.g., Dower et al., 1988, NucleicAcids Res. 16: 6127-6145). The introduction of DNA into a Streptomycescell may be effected by protoplast transformation, electroporation (see,e.g., Gong et al., 2004, Folia Microbiol. (Praha) 49: 399-405),conjugation (see, e.g., Mazodier et al., 1989, J. Bacteriol. 171:3583-3585), or transduction (see, e.g., Burke et al., 2001, Proc. Natl.Acad. Sci. USA 98: 6289-6294). The introduction of DNA into aPseudomonas cell may be effected by electroporation (see, e.g., Choi etal., 2006, J. Microbiol. Methods 64: 391-397) or conjugation (see, e.g.,Pinedo and Smets, 2005, Appl. Environ. Microbiol. 71: 51-57). Theintroduction of DNA into a Streptococcus cell may be effected by naturalcompetence (see, e.g., Perry and Kuramitsu, 1981, Infect. Immun. 32:1295-1297), protoplast transformation (see, e.g., Catt and Jollick,1991, Microbios 68: 189-207), electroporation (see, e.g., Buckley etal., 1999, Appl. Environ. Microbiol. 65: 3800-3804), or conjugation(see, e.g., Clewell, 1981, Microbiol. Rev. 45: 409-436). However, anymethod known in the art for introducing DNA into a host cell can beused.

The host cell may also be a eukaryote, such as a mammalian, insect,plant, or fungal cell.

The host cell may be a fungal cell. “Fungi” as used herein includes thephyla Ascomycota, Basidiomycota, Chytridiomycota, and Zygomycota as wellas the Oomycota and all mitosporic fungi (as defined by Hawksworth etal., In, Ainsworth and Bisby's Dictionary of The Fungi, 8th edition,1995, CAB International, University Press, Cambridge, UK).

The fungal host cell may be a yeast cell. “Yeast” as used hereinincludes ascosporogenous yeast (Endomycetales), basidiosporogenousyeast, and yeast belonging to the Fungi Imperfecti (Blastomycetes).Since the classification of yeast may change in the future, for thepurposes of this invention, yeast shall be defined as described inBiology and Activities of Yeast (Skinner, Passmore, and Davenport,editors, Soc. App. Bacteriol. Symposium Series No. 9, 1980).

The yeast host cell may be a Candida, Hansenula, Kluyveromyces, Pichia,Saccharomyces, Schizosaccharomyces, or Yarrowia cell, such as aKluyveromyces lactis, Saccharomyces carlsbergensis, Saccharomycescerevisiae, Saccharomyces diastaticus, Saccharomyces douglasii,Saccharomyces kluyveri, Saccharomyces norbensis, Saccharomycesoviformis, or Yarrowia lipolytica cell.

The fungal host cell may be a filamentous fungal cell. “Filamentousfungi” include all filamentous forms of the subdivision Eumycota andOomycota (as defined by Hawksworth et al., 1995, supra). The filamentousfungi are generally characterized by a mycelial wall composed of chitin,cellulose, glucan, chitosan, mannan, and other complex polysaccharides.Vegetative growth is by hyphal elongation and carbon catabolism isobligately aerobic. In contrast, vegetative growth by yeasts such asSaccharomyces cerevisiae is by budding of a unicellular thallus andcarbon catabolism may be fermentative.

The filamentous fungal host cell may be an Acremonium, Aspergillus,Aureobasidium, Bjerkandera, Ceriporiopsis, Chrysosporium, Coprinus,Coriolus, Cryptococcus, Filibasidium, Fusarium, Humicola, Magnaporthe,Mucor, Myceliophthora, Neocallimastix, Neurospora, Paecilomyces,Penicillium, Phanerochaete, Phlebia, Piromyces, Pleurotus,Schizophyllum, Talaromyces, Thermoascus, Thielavia, Tolypocladium,Trametes, or Trichoderma cell.

For example, the filamentous fungal host cell may be an Aspergillusawamori, Aspergillus foetidus, Aspergillus fumigatus, Aspergillusjaponicus, Aspergillus nidulans, Aspergillus niger, Aspergillus oryzae,Bjerkandera adusta, Ceriporiopsis aneirina, Ceriporiopsis caregiea,Ceriporiopsis gilvescens, Ceriporiopsis pannocinta, Ceriporiopsisrivulosa, Ceriporiopsis subrufa, Ceriporiopsis subvermispora,Chrysosporium inops, Chrysosporium keratinophilum, Chrysosporiumlucknowense, Chrysosporium merdarium, Chrysosporium pannicola,Chrysosporium queenslandicum, Chrysosporium tropicum, Chrysosporiumzonatum, Coprinus cinereus, Coriolus hirsutus, Fusarium bactridioides,Fusarium cerealis, Fusarium crookwellense, Fusarium culmorum, Fusariumgraminearum, Fusarium graminum, Fusarium heterosporum, Fusarium negundi,Fusarium oxysporum, Fusarium reticulatum, Fusarium roseum, Fusariumsambucinum, Fusarium sarcochroum, Fusarium sporotrichioides, Fusariumsulphureum, Fusarium torulosum, Fusarium trichothecioides, Fusariumvenenatum, Humicola insolens, Humicola lanuginosa, Mucor miehei,Myceliophthora thermophila, Neurospora crassa, Penicillium purpurogenum,Phanerochaete chrysosporium, Phlebia radiata, Pleurotus eryngii,Thielavia terrestris, Trametes villosa, Trametes versicolor, Trichodermaharzianum, Trichoderma koningii, Trichoderma longibrachiatum,Trichoderma reesei, or Trichoderma viride cell.

Fungal cells may be transformed by a process involving protoplastformation, transformation of the protoplasts, and regeneration of thecell wall in a manner known per se. Suitable procedures fortransformation of Aspergillus and Trichoderma host cells are describedin EP 238023, Yelton et al., 1984, Proc. Natl. Acad. Sci. USA 81:1470-1474, and Christensen et al., 1988, Bio/Technology 6: 1419-1422.Suitable methods for transforming Fusarium species are described byMalardier et al., 1989, Gene 78: 147-156, and WO 96/00787. Yeast may betransformed using the procedures described by Becker and Guarente, InAbelson, J. N. and Simon, M. I., editors, Guide to Yeast Genetics andMolecular Biology, Methods in Enzymology, Volume 194, pp 182-187,Academic Press, Inc., New York; Ito et al., 1983, J. Bacteriol. 153:163; and Hinnen et al., 1978, Proc. Natl. Acad. Sci. USA 75: 1920.

Methods of Production

The present invention also relates to methods of producing a polypeptideof the present invention, comprising (a) cultivating a cell, which inits wild-type form produces the polypeptide, under conditions conducivefor production of the polypeptide; and optionally, (b) recovering thepolypeptide. The polypeptide may for example be any of the second to thetwenty-eighth aspect of the invention.

In one aspect, the cell is a Penicillium cell. In another aspect, thecell is a Penicillium aurantiogriseum cell. In a further aspect, thecell is a Penicillium oxalicum cell. In a further aspect, the cell is aPenicillium capsulatum cell. In a further aspect, the cell is aPenicillium soppii cell. In one aspect, the cell is an Aspergillus cell.In another aspect, the cell is an Aspergillus clavatus cell. In afurther aspect, the cell is an Aspergillus wentii cell. In a furtheraspect, the cell is an Aspergillus aculeatus cell. In a further aspect,the cell is an Aspergillus fumigatiaffinis cell.

In one aspect, the cell is a Neosartorya cell. In another aspect, thecell is a Neosartorya fischeri cell. In one aspect, the cell is aTalaromyces cell. In another aspect, the cell is a Talaromycespinophilus cell. In one aspect, the cell is a Ustilago cell. In anotheraspect, the cell is a Ustilago maydis cell. In one aspect, the cell isan Acrophialophora cell. In another aspect, the cell is anAcrophialophora fusispora cell. In one aspect, the cell is aStreptomyces cell. In another aspect, the cell is a Streptomycesnitrosporeus cell. In a further aspect, the cell is a Streptomycesbeijiangensis cell. In one aspect, the cell is a Streptosporangium cell.In another aspect, the cell is a Streptosporangium sp-60756 cell.

In one aspect, the cell is a Lasiodiplodia cell. In another aspect, thecell is a Lasiodiplodia theobromae cell. In one aspect, the cell is anAscobolus cell. In another aspect, the cell is a Ascobolus stictoideuscell. In one aspect, the cell is a Drechslera cell. In another aspect,the cell is a Drechslera sp cell. In one aspect, the cell is aXylanibacterium cell. In another aspect, the cell is a Xylanibacteriumsp-61981 cell. In one aspect, the cell is a Microdochium cell. Inanother aspect, the cell is a Microdochium nivale cell. In one aspect,the cell is a Humicola cell. In another aspect, the cell is a Humicolahyalothermophila cell. In another aspect, the cell is a Humicola spcell.

In one aspect, the cell is a Curvularia cell. In another aspect, thecell is a Curvularia geniculata cell. In one aspect, the cell is aGlycomyces cell. In another aspect, the cell is a Glycomycesrutgersensis cell. In one aspect, the cell is a Remersonia cell. Inanother aspect, the cell is a Remersonia thermophile cell. In oneaspect, the cell is a Thielavia cell. In another aspect, the cell is aThielavia arenaria cell. In another aspect, the cell is a Thielaviaterricola cell. In one aspect, the cell is a Chaetomium cell. In anotheraspect, the cell is a Chaetomium olivicolor cell.

The present invention also relates to methods of producing a polypeptideof the present invention, comprising (a) cultivating a recombinant hostcell of the present invention under conditions conducive for productionof the polypeptide; and optionally, (b) recovering the polypeptide. Thepolypeptide may for example be any of the second to the twenty-eighthaspect of the invention.

The host cells are cultivated in a nutrient medium suitable forproduction of the polypeptide using methods known in the art. Forexample, the cells may be cultivated by shake flask cultivation, orsmall-scale or large-scale fermentation (including continuous, batch,fed-batch, or solid state fermentations) in laboratory or industrialfermentors in a suitable medium and under conditions allowing thepolypeptide to be expressed and/or isolated. The cultivation takes placein a suitable nutrient medium comprising carbon and nitrogen sources andinorganic salts, using procedures known in the art. Suitable media areavailable from commercial suppliers or may be prepared according topublished compositions (e.g., in catalogues of the American Type CultureCollection). If the polypeptide is secreted into the nutrient medium,the polypeptide can be recovered directly from the medium. If thepolypeptide is not secreted, it can be recovered from cell lysates.

The polypeptide may be detected using methods known in the art that arespecific for the polypeptides. These detection methods include, but arenot limited to, use of specific antibodies, formation of an enzymeproduct, or disappearance of an enzyme substrate. For example, an enzymeassay may be used to determine the activity of the polypeptide.

The polypeptide may be recovered using methods known in the art. Forexample, the polypeptide may be recovered from the nutrient medium byconventional procedures including, but not limited to, collection,centrifugation, filtration, extraction, spray-drying, evaporation, orprecipitation. In one aspect, a fermentation broth comprising thepolypeptide is recovered.

The polypeptide may be purified by a variety of procedures known in theart including, but not limited to, chromatography (e.g., ion exchange,affinity, hydrophobic, chromatofocusing, and size exclusion),electrophoretic procedures (e.g., preparative isoelectric focusing),differential solubility (e.g., ammonium sulfate precipitation),SDS-PAGE, or extraction (see, e.g., Protein Purification, Janson andRyden, editors, VCH Publishers, New York, 1989) to obtain substantiallypure polypeptides.

In an alternative aspect, the polypeptide is not recovered, but rather ahost cell of the present invention expressing the polypeptide is used asa source of the polypeptide.

Fermentation Broth Formulations or Cell Compositions

The present invention also relates to a fermentation broth formulationor a cell composition comprising a polypeptide of the present invention.The fermentation broth product further comprises additional ingredientsused in the fermentation process, such as, for example, cells(including, the host cells containing the gene encoding the polypeptideof the present invention which are used to produce the polypeptide ofinterest), cell debris, biomass, fermentation media and/or fermentationproducts. In some embodiments, the composition is a cell-killed wholebroth containing organic acid(s), killed cells and/or cell debris, andculture medium.

The term “fermentation broth” as used herein refers to a preparationproduced by cellular fermentation that undergoes no or minimal recoveryand/or purification. For example, fermentation broths are produced whenmicrobial cultures are grown to saturation, incubated undercarbon-limiting conditions to allow protein synthesis (e.g., expressionof enzymes by host cells) and secretion into cell culture medium. Thefermentation broth can contain unfractionated or fractionated contentsof the fermentation materials derived at the end of the fermentation.Typically, the fermentation broth is unfractionated and comprises thespent culture medium and cell debris present after the microbial cells(e.g., filamentous fungal cells) are removed, e.g., by centrifugation.In some embodiments, the fermentation broth contains spent cell culturemedium, extracellular enzymes, and viable and/or nonviable microbialcells.

In an embodiment, the fermentation broth formulation and cellcompositions comprise a first organic acid component comprising at leastone 1-5 carbon organic acid and/or a salt thereof and a second organicacid component comprising at least one 6 or more carbon organic acidand/or a salt thereof. In a specific embodiment, the first organic acidcomponent is acetic acid, formic acid, propionic acid, a salt thereof,or a mixture of two or more of the foregoing and the second organic acidcomponent is benzoic acid, cyclohexanecarboxylic acid, 4-methylvalericacid, phenylacetic acid, a salt thereof, or a mixture of two or more ofthe foregoing.

In one aspect, the composition contains an organic acid(s), andoptionally further contains killed cells and/or cell debris. In oneembodiment, the killed cells and/or cell debris are removed from acell-killed whole broth to provide a composition that is free of thesecomponents.

The fermentation broth formulations or cell compositions may furthercomprise a preservative and/or anti-microbial (e.g., bacteriostatic)agent, including, but not limited to, sorbitol, sodium chloride,potassium sorbate, and others known in the art.

The cell-killed whole broth or composition may contain theunfractionated contents of the fermentation materials derived at the endof the fermentation. Typically, the cell-killed whole broth orcomposition contains the spent culture medium and cell debris presentafter the microbial cells (e.g., filamentous fungal cells) are grown tosaturation, incubated under carbon-limiting conditions to allow proteinsynthesis. In some embodiments, the cell-killed whole broth orcomposition contains the spent cell culture medium, extracellularenzymes, and killed filamentous fungal cells. In some embodiments, themicrobial cells present in the cell-killed whole broth or compositioncan be permeabilized and/or lysed using methods known in the art.

A whole broth or cell composition as described herein is typically aliquid, but may contain insoluble components, such as killed cells, celldebris, culture media components, and/or insoluble enzyme(s). In someembodiments, insoluble components may be removed to provide a clarifiedliquid composition.

The whole broth formulations and cell compositions of the presentinvention may be produced by a method described in WO 90/15861 or WO2010/096673.

Enzyme Compositions

Preferably, the compositions are enriched in the polypeptides of thefirst aspect of the invention. The term “enriched” indicates that thearabinofuranosidase activity and the xylanase activity of thecomposition has been increased, e.g., with an enrichment factor of atleast 1.1, such as at least 1.2, at least 1.3, at least 1.4, at least1.5, at least 2.0, at least 3.0, at least 4.0, at least 5.0, at least10. In an embodiment, the composition comprises the polypeptides of thefirst aspect of the invention and one or more formulating agents, asdescribed in the ‘formulating agent’ section below.

The present invention also relates to compositions comprising thepolypeptide of any of the second to the twenty-fifth aspect of theinvention having arabinofuranosidase activity. Preferably, thecompositions are enriched in the polypeptide of the second aspect of theinvention. The term “enriched” indicates that the arabinofuranosidaseactivity of the composition has been increased, e.g., with an enrichmentfactor of at least 1.1, such as at least 1.2, at least 1.3, at least1.4, at least 1.5, at least 2.0, at least 3.0, at least 4.0, at least5.0, at least 10. In an embodiment, the composition comprises thepolypeptide of the second aspect of the invention and one or moreformulating agents, as described in the ‘formulating agent’ sectionbelow. In a further embodiment, the composition further comprises one ormore GH10 or GH11 polypeptides having xylanase activity.

The present invention also relates to compositions comprising thepolypeptide of any of the twenty-sixth to the twenty-eighth aspect ofthe invention having xylanase activity. Preferably, the compositions areenriched in the polypeptide of the second aspect of the invention. Theterm “enriched” indicates that the arabinofuranosidase activity of thecomposition has been increased, e.g., with an enrichment factor of atleast 1.1, such as at least 1.2, at least 1.3, at least 1.4, at least1.5, at least 2.0, at least 3.0, at least 4.0, at least 5.0, at least10. In an embodiment, the composition comprises the polypeptide of thesecond aspect of the invention and one or more formulating agents, asdescribed in the ‘formulating agent’ section below. In a furtherembodiment, the composition further comprises one or more GH62polypeptides having arabinofuranosidase activity.

The compositions may comprise a polypeptide of the present invention asthe major enzymatic component, e.g., a mono-component composition. Sucha composition may further comprise a formulating agent, as described inthe ‘formulating agent’ section below. Alternatively, the compositionsmay comprise multiple enzymatic activities, such as one or more (e.g.,several) enzymes selected from the group consisting of phytase,xylanase, galactanase, alpha-galactosidase, protease, phospholipase,glucoronidase, lysophospholipase, amylase, beta-glucanase,arabinofuranosidase, beta-xylosidase, endo-1,4-beta-xylanase acetylxylan esterase, feruloyl esterase, cellulase, cellobiohydrolase,beta-glycosidase, pullulanase, or any mixture thereof.

It is at present contemplated that the xylanase is used in one or moreof the following amounts (dosage ranges): 0.01-200; 0.05-100; 0.1-50;0.2-20; 0.1-1; 0.2-2; 0.5-5; or 1-10 wherein all these ranges are mgxylanase protein per kg substrate (ppm). It is at present contemplatedthat the arabinofuranosidase is administered in one or more of thefollowing amounts (dosage ranges): 0.01-200; 0.05-100; 0.1-50; 0.2-20;0.1-1; 0.2-2; 0.5-5; or 1-10 wherein all these ranges are mgarabinofuranosidase protein per kg substrate (ppm). It is furthercontemplated that the ratio of the GH10 or 11 xylanase to GH62arabinofuranosidase is in the range of 100:1 to 1:100 xylanase:arabinofuranosidase such as the ranges 50:1 to 1:50, 50:1 to 1:10, 25:1to 1:5, 10:1 to 1:2 or such as 10:1 to 1:50, 5:1 to 1:25, 2:1 to 1:10xylanase: arabinofuranosidase.

Formulating Agent

The enzyme of the invention may be formulated as a liquid or a solid.For a liquid formulation, the formulating agent may comprise a polyol(such as e.g. glycerol, ethylene glycol or propylene glycol), a salt(such as e.g. sodium chloride, sodium benzoate, potassium sorbate) or asugar or sugar derivative (such as e.g. dextrin, glucose, sucrose, andsorbitol). Thus in one embodiment, the composition is a liquidcomposition comprising the polypeptide of the invention and one or moreformulating agents selected from the list consisting of glycerol,ethylene glycol, 1,2-propylene glycol, 1,3-propylene glycol, sodiumchloride, sodium benzoate, potassium sorbate, dextrin, glucose, sucrose,and sorbitol.

For a solid formulation, the formulation may be for example as agranule, spray dried powder or agglomerate. The formulating agent maycomprise a salt (organic or inorganic zinc, sodium, potassium or calciumsalts such as e.g. such as calcium acetate, calcium benzoate, calciumcarbonate, calcium chloride, calcium citrate, calcium sorbate, calciumsulfate, potassium acetate, potassium benzoate, potassium carbonate,potassium chloride, potassium citrate, potassium sorbate, potassiumsulfate, sodium acetate, sodium benzoate, sodium carbonate, sodiumchloride, sodium citrate, sodium sulfate, zinc acetate, zinc benzoate,zinc carbonate, zinc chloride, zinc citrate, zinc sorbate, zincsulfate), starch or a sugar or sugar derivative (such as e.g. sucrose,dextrin, glucose, lactose, sorbitol).

In an embodiment, the solid composition is in granulated form. Thegranule may have a matrix structure where the components are mixedhomogeneously. However, the granule typically comprises a core particleand one or more coatings, which typically are salt and/or wax coatings.The core particle can either be a homogeneous blend of xylanase of theinvention optionally combined with one or more additional enzymes andoptionally together with one or more salts or an inert particle with thexylanase of the invention optionally combined with one or moreadditional enzymes applied onto it.

In an embodiment, the material of the core particles are selected fromthe group consisting of inorganic salts (such as calcium acetate,calcium benzoate, calcium carbonate, calcium chloride, calcium citrate,calcium sorbate, calcium sulfate, potassium acetate, potassium benzoate,potassium carbonate, potassium chloride, potassium citrate, potassiumsorbate, potassium sulfate, sodium acetate, sodium benzoate, sodiumcarbonate, sodium chloride, sodium citrate, sodium sulfate, zincacetate, zinc benzoate, zinc carbonate, zinc chloride, zinc citrate,zinc sorbate, zinc sulfate), starch or a sugar or sugar derivative (suchas e.g. sucrose, dextrin, glucose, lactose, sorbitol), sugar or sugarderivative (such as e.g. sucrose, dextrin, glucose, lactose, sorbitol),small organic molecules, starch, flour, cellulose and minerals.

The salt coating is typically at least 1 μm thick and can either be oneparticular salt or a mixture of salts, such as Na₂SO₄, K₂SO₄, MgSO₄and/or sodium citrate. Other examples are those described in e.g. WO2008/017659, WO 2006/034710, WO 1997/05245, WO 1998/54980, WO1998/55599, WO 2000/70034 or polymer coating such as described in WO2001/00042.

In another embodiment, the composition is a solid composition comprisingthe xylanase of the invention and one or more formulating agentsselected from the list consisting of sodium chloride, sodium benzoate,potassium sorbate, sodium sulfate, potassium sulfate, magnesium sulfate,sodium thiosulfate, calcium carbonate, sodium citrate, dextrin, glucose,sucrose, sorbitol, lactose, starch and cellulose. In a preferredembodiment, the formulating agent is selected from one or more of thefollowing compounds: sodium sulfate, dextrin, cellulose, sodiumthiosulfate and calcium carbonate. In a preferred embodiment, the solidcomposition is in granulated form. In an embodiment, the solidcomposition is in granulated form and comprises a core particle, anenzyme layer comprising the xylanase of the invention and a saltcoating.

In a further embodiment, the formulating agent is selected from one ormore of the following compounds: glycerol, ethylene glycol,1,2-propylene glycol or 1,3-propylene glycol, sodium chloride, sodiumbenzoate, potassium sorbate, sodium sulfate, potassium sulfate,magnesium sulfate, sodium thiosulfate, calcium carbonate, sodiumcitrate, dextrin, glucose, sucrose, sorbitol, lactose, starch andcellulose. In a preferred embodiment, the formulating agent is selectedfrom one or more of the following compounds: 1,2-propylene glycol,1,3-propylene glycol, sodium sulfate, dextrin, cellulose, sodiumthiosulfate and calcium carbonate.

Plant Based Material from the Sub-Family Panicoideae

In one embodiment, the plant based material from the sub-familyPanicoideae is from the tribe Andropogoneae such as the rank Andropogonor Andropterum or Apluda or Apocopis or Arthraxon or Bothriochloa orCapillipedium or Chionachne or Chrysopogon or Coelorachis or Coix orCymbopogon or Dichanthium or Diheteropogon or Dimeria or Elionurus orEremochloa or Euclasta or Eulalia or Germainia or Hemarthria orHeteropholis or Heteropogon or Hyparrhenia or Hyperthelia or Imperata orIschaemum or Iseilema or Kerriochloa or Microstegium or Miscanthidium orMiscanthus or Mnesithea or Ophiuros or Oxyrhachis or Phacelurus orPholiurus or Pogonatherum or Polytoca or Polytrias or Pseudopogonatherumor Pseudosorghum or Rhytachne or Rottboellia or Saccharum or Sarga orSchizachyrium or Sehima or Sorghastrum or Sorghum or Spodiopogon orThaumastochloa or Thelepogon or Themeda or Trachypogon or Triarrhena orTripsacum or Urelytrum or Vetiveria or Vossia or Xerochloa or Zea.

In a preferred embodiment, the plant based material from the sub-familyPanicoideae is from the rank Zea, such as the species Zea diploperennis,Zea luxurians, Zea mays, Zea nicaraguensis or Zea perennis.

In a preferred embodiment, the plant based material from the sub-familyPanicoideae is from the rank Sorghum, such as the species Sorghumamplum, Sorghum angustum, Sorghum arundinaceum, Sorghum australiense,Sorghum bicolor, Sorghum brachypodum, Sorghum bulbosum, Sorghumecarinatum, Sorghum exstans, Sorghum grande, Sorghum halepense, Sorghumhybrid cultivar, Sorghum interjectum, Sorghum intrans, Sorghumlaxiflorum, Sorghum leiocladum, Sorghum macrospermum, Sorghummatarankense, Sorghum nitidum, Sorghum plumosum, Sorghum propinquum,Sorghum purpureosericeum, Sorghum stipoideum, Sorghum sudanense, Sorghumtimorense, Sorghum versicolor, Sorghum sp. ‘Silk’ or Sorghum sp. asdefined in WO2007/002267.

In another embodiment, the plant based material from the sub-familyPanicoideae is from the tribe Paniceae such as the rank Acritochaete,Acroceras, Alexfloydia, Alloteropsis, Amphicarpum, Ancistrachne,Anthephora, Brachiaria, Calyptochloa, Cenchrus, Chaetium, Chaetopoa,Chamaeraphis, Chlorocalymma, Cleistochloa, Cyphochlaena, Cyrtococcum,Dichanthelium, Digitaria, Dissochondrus, Echinochloa, Entolasia,Eriochloa, Homopholis, Hygrochloa, Hylebates, Ixophorus, Lasiacis,Leucophrys, Louisiella, Megaloprotachne, Megathyrsus, Melinis,Microcalamus, Moorochloa, Neurachne, Odontelytrum, Oplismenus,Ottochloa, Panicum, Paractaenum, Paraneurachne, Paratheria,Parodiophyllochloa, Paspalidium, Pennisetum, Plagiosetum,Poecilostachys, Pseudechinolaena, Pseudochaetochloa, Pseudoraphis,Rupichloa, Sacciolepis, Scutachne, Setaria, Setariopsis, Snowdenia,Spinifex, Stenotaphrum, Stereochlaena, Thrasya, Thuarea, Thyridolepis,Tricholaena, unclassified Paniceae, Uranthoecium, Urochloa, Walwhalleya,Whiteochloa, Yakirra, Yvesia, Zuloagaea or Zygochloa.

In a preferred embodiment, the plant based material from the sub-familyPanicoideae is from the rank Panicum, such as the species Panicumadenophorum, Panicum aff. aquaticum JKT-2012, Panicum amarum, Panicumantidotale, Panicum aquaticum, Panicum arctum, Panicum arundinariae,Panicum atrosanguineum, Panicum auricomum, Panicum auritum, Panicumbartlettii, Panicum bergii, Panicum bisulcatum, Panicum boliviense,Panicum brazzavillense, Panicum brevifolium, Panicum caaguazuense,Panicum campestre, Panicum capillare, Panicum cayennense, Panicumcayoense, Panicum cervicatum, Panicum chloroleucum, Panicum claytonii,Panicum coloratum, Panicum cyanescens, Panicum decompositum, Panicumdeustum, Panicum dichotomiflorum, Panicum dinklagei, Panicumdistichophyllum, Panicum dregeanum, Panicum elephantipes, Panicumfauriei, Panicum flexile, Panicum fluviicola, Panicum gouinii, Panicumgracilicaule, Panicum granuliferum, Panicum guatemalense, Panicumhallii, Panicum heterostachyum, Panicum hirticaule, Panicum hirtum,Panicum hylaeicum, Panicum incumbens, Panicum infestum, Panicumitalicum, Panicum laetum, Panicum laevinode, Panicum lanipes, Panicumlarcomianum, Panicum longpedicellatum, Panicum machrisianum, Panicummalacotrichum, Panicum margaritiferum, Panicum micranthum, Panicummiliaceum, Panicum milioides, Panicum millegrana, Panicum mystasipum,Panicum natalense, Panicum nephelophilum, Panicum nervosum, Panicumnotatum, Panicum olyroides, Panicum paludosum, Panicum pansum, Panicumpantrichum, Panicum parvifolium, Panicum parviglume, Panicum pedersenii,Panicum penicillatum, Panicum petersonii, Panicum phragmitoides, Panicumpiauiense, Panicum pilosum, Panicum pleianthum, Panicum polycomum,Panicum polygonatum, Panicum pseudisachne, Panicum pygmaeum, Panicumpyrularium, Panicum queenslandicum, Panicum racemosum, Panicum repens,Panicum rhizogonum, Panicum rigidulum, Panicum rivale, Panicum rude,Panicum rudgei, Panicum schinzii, Panicum schwackeanum, Panicumsellowii, Panicum seminudum, Panicum stapfianum, Panicum stenodes,Panicum stramineum, Panicum subalbidum, Panicum subtiramulosum, Panicumsumatrense, Panicum tenellum, Panicum tenuifolium, Panicum trichanthum,Panicum trichidiachne, Panicum trichoides, Panicum tricholaenoides,Panicum tuerckheimii, Panicum turgidum, Panicum urvilleanum, Panicumvalidum, Panicum venezuelae, Panicum verrucosum, Panicum virgatum,Panicum wettsteinii, Panicum sp., Panicum sp. Christin 16-200, Panicumsp. ELS-2011, Panicum sp. EM389 or Panicum sp. Forest 761.

In a further embodiment, the plant based material from the sub-familyPanicoideae is maize (Zea), corn (Zea), sorghum (Sorghum), switchgrass(Panicum virgatum), millet (Panicum miliaceum), pearl millet (Cenchrusviolaceus also called Pennisetum glaucum), foxtail millet (Setariaitalica also called Panicum italicum) or in a processed form such asmilled corn, milled maize, defatted maize, defatted destarched maize,milled sorghum, milled switchgrass, milled millet, milled foxtailmillet, milled pearl millet, or any combination thereof.

In an embodiment, the plant based material from the sub-familyPanicoideae is from the seed of the plant. In a preferred embodiment,the plant based material from the sub-family Panicoideae is from theseed of maize (Zea), corn (Zea), sorghum (Sorghum), switchgrass (Panicumvirgatum), millet (Panicum miliaceum), pearl millet (Cenchrus violaceusalso called Pennisetum glaucum), foxtail millet (Setaria italica alsocalled Panicum italicum) or wherein the seed has been processed such asmilled corn, milled maize, defatted maize, defatted destarched maize,milled sorghum, milled switchgrass, milled millet, milled foxtailmillet, milled pearl millet, or any combination thereof.

Animal Feed and Animal Feed Additives

The present invention also relates to animal feeds and animal feedadditives comprising the composition of the first aspect of theinvention. In an embodiment, the animal feed additive comprises aformulating agent and the composition of the first aspect of theinvention. In an embodiment, the animal feed comprises a formulatingagent and the composition of the first aspect of the invention. In afurther embodiment, the formulating agent comprises one or more of thefollowing compounds: glycerol, ethylene glycol, 1,2-propylene glycol or1,3-propylene glycol, sodium chloride, sodium benzoate, potassiumsorbate, sodium sulfate, potassium sulfate, magnesium sulfate, sodiumthiosulfate, calcium carbonate, sodium citrate, dextrin, glucose,sucrose, sorbitol, lactose, starch and cellulose.

In an embodiment, the animal feed or animal feed additive comprises oneor more additional enzymes. In an embodiment, the animal feed or animalfeed additive comprises one or more microbes. In an embodiment, theanimal feed or animal feed additive comprises one or more vitamins. Inan embodiment, the animal feed or animal feed additive comprises one ormore minerals. In an embodiment, the animal feed or animal feed additivecomprises one or more amino acids. In a further embodiment, the animalfeed or animal feed additive further comprises one or more formulatingagents and one or more components selected from the list consisting of:one or more additional enzymes; one or more microbes; one or morevitamins; one or more minerals; one or more amino acids; and one or moreother feed ingredients.

The present invention also relates to animal feeds and animal feedadditives comprising the polypeptide of any of the second to thetwenty-eighth aspect of the invention. In an embodiment, the animal feedor animal feed additive comprises a formulating agent and one or morepolypeptides any of the second to the twenty-eighth aspect of theinvention. In a further embodiment, the formulating agent comprises oneor more of the following compounds: glycerol, ethylene glycol,1,2-propylene glycol or 1,3-propylene glycol, sodium chloride, sodiumbenzoate, potassium sorbate, sodium sulfate, potassium sulfate,magnesium sulfate, sodium thiosulfate, calcium carbonate, sodiumcitrate, dextrin, glucose, sucrose, sorbitol, lactose, starch andcellulose. In an embodiment, the animal feed or animal feed additivecomprises one or more additional enzymes. In a preferred embodiment, theanimal feed or animal feed additive further comprises one or more GH10or GH11 polypeptides having xylanase activity. In an embodiment, theanimal feed or animal feed additive comprises one or more microbes. Inan embodiment, the animal feed or animal feed additive comprises one ormore vitamins. In an embodiment, the animal feed or animal feed additivecomprises one or more minerals. In an embodiment, the animal feed oranimal feed additive comprises one or more amino acids. In a furtherembodiment, the animal feed or animal feed additive further comprisesone or more formulating agents and one or more components selected fromthe list consisting of: one or more additional enzymes; one or moremicrobes; one or more vitamins; one or more minerals; one or more aminoacids; and one or more other feed ingredients.

The present invention also relates to an animal feed or an animal feedadditive comprising a polypeptide having xylanase activity and having atleast 80% sequence identity, e.g., at least 85%, at least 86%, at least87%, at least 88%, at least 89%, at least 90%, at least 91%, at least92%, at least 93%, at least 94%, at least 95%, at least 96%, at least97%, at least 98% or at least 99% to the polypeptide of SEQ ID NO: 71.In one embodiment, the polypeptides differ by up to 25 amino acids,e.g., between 1 and 25 amino acids, such as 1-25, 1-20, 1-15, 1-10 or1-5 amino acids, or 1, 2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, 15,16, 17, 18, 19, 20, 21, 22, 23, 24 or 25 amino acids from SEQ ID NO: 71.In an embodiment, the animal feed or animal feed additive furthercomprises a formulating agent as described in the formulating agentsection above. In a further embodiment, the formulating agent comprisesone or more of the following compounds: glycerol, ethylene glycol,1,2-propylene glycol or 1,3-propylene glycol, sodium chloride, sodiumbenzoate, potassium sorbate, sodium sulfate, potassium sulfate,magnesium sulfate, sodium thiosulfate, calcium carbonate, sodiumcitrate, dextrin, glucose, sucrose, sorbitol, lactose, starch andcellulose. In an embodiment, the animal feed or animal feed additivecomprises one or more additional enzymes. In a preferred embodiment, theanimal feed or animal feed additive further comprises one or more GH62polypeptides having arabinofuranosidase activity. In an embodiment, theanimal feed or animal feed additive comprises one or more microbes. Inan embodiment, the animal feed or animal feed additive comprises one ormore vitamins. In an embodiment, the animal feed or animal feed additivecomprises one or more minerals. In an embodiment, the animal feed oranimal feed additive comprises one or more amino acids. In a furtherembodiment, the animal feed or animal feed additive further comprisesone or more formulating agents and one or more components selected fromthe list consisting of: one or more additional enzymes; one or moremicrobes; one or more vitamins; one or more minerals; one or more aminoacids; and one or more other feed ingredients.

In one embodiment, the animal feed or an animal feed additive comprisesa polypeptide comprising or consisting of the amino acid sequence of SEQID NO: 71 or an allelic variant thereof; or is a fragment thereof havingxylanase activity and having at least 90% such as at least 91%, at least92%, at least 93%, at least 94%, at least 95%, at least 96%, at least97%, at least 98% or at least 99% of the length of the polypeptide. Inanother embodiment, animal feed or an animal feed additive comprises apolypeptide comprising or consisting of amino acids 1 to 288 of SEQ IDNO: 71.

In another embodiment, the animal feed or an animal feed additivecomprises a variant polypeptide having xylanase activity wherein thepolypeptide is a variant of SEQ ID NO: 71 comprising one or more aminoacid substitutions, and/or one or more amino acid deletions, and/or oneor more amino acid insertions or any combination thereof in 1, 2, 3, 4,5, 6, 7, 8, 9, 10, 11, 12, 13, 14, 15, 16, 17, 18, 19, 20, 21, 22, 23,24 or 25 positions. In an embodiment, the number of positions comprisingone or more amino acid substitutions, and/or one or more amino aciddeletions, and/or one or more amino acid insertions or any combinationthereof in SEQ ID NO: 71 is not more than 10, e.g., 1, 2, 3, 4, 5, 6, 7,8, 9 or 10. In another embodiment, the number of substitutions,deletions, and/or insertions in SEQ ID NO: 71 is not more than 10, e.g.,1, 2, 3, 4, 5, 6, 7, 8, 9 or 10. In a further embodiment, the number ofsubstitutions, preferably conservative substitutions, in SEQ ID NO: 71is not more than 10, e.g., 1, 2, 3, 4, 5, 6, 7, 8, 9 or 10. Examples ofamino acid changes and conservative substitutions are described in thesecond aspect of the invention.

The present invention also relates to an animal feed or an animal feedadditive comprising a polypeptide having xylanase activity and having atleast 80% sequence identity, e.g., at least 85%, at least 86%, at least87%, at least 88%, at least 89%, at least 90%, at least 91%, at least92%, at least 93%, at least 94%, at least 95%, at least 96%, at least97%, at least 98% or at least 99% to the polypeptide of SEQ ID NO: 78.In one embodiment, the polypeptides differ by up to 25 amino acids,e.g., between 1 and 25 amino acids, such as 1-25, 1-20, 1-15, 1-10 or1-5 amino acids, or 1, 2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, 15,16, 17, 18, 19, 20, 21, 22, 23, 24 or 25 amino acids from SEQ ID NO: 78.In an embodiment, the animal feed or animal feed additive furthercomprises a formulating agent as described in the formulating agentsection above. In a further embodiment, the formulating agent comprisesone or more of the following compounds: glycerol, ethylene glycol,1,2-propylene glycol or 1,3-propylene glycol, sodium chloride, sodiumbenzoate, potassium sorbate, sodium sulfate, potassium sulfate,magnesium sulfate, sodium thiosulfate, calcium carbonate, sodiumcitrate, dextrin, glucose, sucrose, sorbitol, lactose, starch andcellulose. In an embodiment, the animal feed or animal feed additivecomprises one or more additional enzymes. In a preferred embodiment, theanimal feed or animal feed additive further comprises one or more GH62polypeptides having arabinofuranosidase activity. In an embodiment, theanimal feed or animal feed additive comprises one or more microbes. Inan embodiment, the animal feed or animal feed additive comprises one ormore vitamins. In an embodiment, the animal feed or animal feed additivecomprises one or more minerals. In an embodiment, the animal feed oranimal feed additive comprises one or more amino acids. In a furtherembodiment, the animal feed or animal feed additive further comprisesone or more formulating agents and one or more components selected fromthe list consisting of: one or more additional enzymes; one or moremicrobes; one or more vitamins; one or more minerals; one or more aminoacids; and one or more other feed ingredients.

In one embodiment, the animal feed or an animal feed additive comprisesa polypeptide comprising or consisting of the amino acid sequence of SEQID NO: 78 or an allelic variant thereof; or is a fragment thereof havingxylanase activity and having at least 90% such as at least 91%, at least92%, at least 93%, at least 94%, at least 95%, at least 96%, at least97%, at least 98% or at least 99% of the length of the polypeptide. Inanother embodiment, animal feed or an animal feed additive comprises apolypeptide comprising or consisting of amino acids 1 to 183 of SEQ IDNO: 78. In another embodiment, animal feed or an animal feed additivecomprises a polypeptide comprising or consisting of amino acids 1 to 181of SEQ ID NO: 81.

In another embodiment, the animal feed or an animal feed additivecomprises a variant polypeptide having xylanase activity wherein thepolypeptide is a variant of SEQ ID NO: 78 comprising one or more aminoacid substitutions, and/or one or more amino acid deletions, and/or oneor more amino acid insertions or any combination thereof in 1, 2, 3, 4,5, 6, 7, 8, 9, 10, 11, 12, 13, 14, 15, 16, 17, 18, 19, 20, 21, 22, 23,24 or 25 positions. In an embodiment, the number of positions comprisingone or more amino acid substitutions, and/or one or more amino aciddeletions, and/or one or more amino acid insertions or any combinationthereof in SEQ ID NO: 78 is not more than 10, e.g., 1, 2, 3, 4, 5, 6, 7,8, 9 or 10. In another embodiment, the number of substitutions,deletions, and/or insertions in SEQ ID NO: 78 is not more than 10, e.g.,1, 2, 3, 4, 5, 6, 7, 8, 9 or 10. In a further embodiment, the number ofsubstitutions, preferably conservative substitutions, in SEQ ID NO: 78is not more than 10, e.g., 1, 2, 3, 4, 5, 6, 7, 8, 9 or 10. Examples ofamino acid changes and conservative substitutions are described in thesecond aspect of the invention.

The present invention also relates to an animal feed or an animal feedadditive comprising a polypeptide having xylanase activity and having atleast 80% sequence identity, e.g., at least 85%, at least 86%, at least87%, at least 88%, at least 89%, at least 90%, at least 91%, at least92%, at least 93%, at least 94%, at least 95%, at least 96%, at least97%, at least 98% or at least 99% to the polypeptide of SEQ ID NO: 177.In one embodiment, the polypeptides differ by up to 25 amino acids,e.g., between 1 and 25 amino acids, such as 1-25, 1-20, 1-15, 1-10 or1-5 amino acids, or 1, 2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, 15,16, 17, 18, 19, 20, 21, 22, 23, 24 or 25 amino acids from SEQ ID NO:177. In an embodiment, the animal feed or animal feed additive furthercomprises a formulating agent as described in the formulating agentsection above. In a further embodiment, the formulating agent comprisesone or more of the following compounds: glycerol, ethylene glycol,1,2-propylene glycol or 1,3-propylene glycol, sodium chloride, sodiumbenzoate, potassium sorbate, sodium sulfate, potassium sulfate,magnesium sulfate, sodium thiosulfate, calcium carbonate, sodiumcitrate, dextrin, glucose, sucrose, sorbitol, lactose, starch andcellulose. In an embodiment, the animal feed or animal feed additivecomprises one or more additional enzymes. In a preferred embodiment, theanimal feed or animal feed additive further comprises one or more GH62polypeptides having arabinofuranosidase activity. In an embodiment, theanimal feed or animal feed additive comprises one or more microbes. Inan embodiment, the animal feed or animal feed additive comprises one ormore vitamins. In an embodiment, the animal feed or animal feed additivecomprises one or more minerals. In an embodiment, the animal feed oranimal feed additive comprises one or more amino acids. In a furtherembodiment, the animal feed or animal feed additive further comprisesone or more formulating agents and one or more components selected fromthe list consisting of: one or more additional enzymes; one or moremicrobes; one or more vitamins; one or more minerals; one or more aminoacids; and one or more other feed ingredients.

In one embodiment, the animal feed or an animal feed additive comprisesa polypeptide comprising or consisting of the amino acid sequence of SEQID NO: 177 or an allelic variant thereof; or is a fragment thereofhaving xylanase activity and having at least 90% such as at least 91%,at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, atleast 97%, at least 98% or at least 99% of the length of thepolypeptide. In another embodiment, animal feed or an animal feedadditive comprises a polypeptide comprising or consisting of amino acids1 to 323 of SEQ ID NO: 177. In another embodiment, animal feed or ananimal feed additive comprises a polypeptide comprising or consisting ofamino acids 1 to 331 of SEQ ID NO: 180.

In another embodiment, the animal feed or an animal feed additivecomprises a variant polypeptide having xylanase activity wherein thepolypeptide is a variant of SEQ ID NO: 177 comprising one or more aminoacid substitutions, and/or one or more amino acid deletions, and/or oneor more amino acid insertions or any combination thereof in 1, 2, 3, 4,5, 6, 7, 8, 9, 10, 11, 12, 13, 14, 15, 16, 17, 18, 19, 20, 21, 22, 23,24 or 25 positions. In an embodiment, the number of positions comprisingone or more amino acid substitutions, and/or one or more amino aciddeletions, and/or one or more amino acid insertions or any combinationthereof in SEQ ID NO: 177 is not more than 10, e.g., 1, 2, 3, 4, 5, 6,7, 8, 9 or 10. In another embodiment, the number of substitutions,deletions, and/or insertions in SEQ ID NO: 177 is not more than 10,e.g., 1, 2, 3, 4, 5, 6, 7, 8, 9 or 10. In a further embodiment, thenumber of substitutions, preferably conservative substitutions, in SEQID NO: 177 is not more than 10, e.g., 1, 2, 3, 4, 5, 6, 7, 8, 9 or 10.Examples of amino acid changes and conservative substitutions aredescribed in the second aspect of the invention.

The present invention also relates to an animal feed or an animal feedadditive comprising a polypeptide having arabinofuranosidase activityand having at least 80% sequence identity, e.g., at least 85%, at least86%, at least 87%, at least 88%, at least 89%, at least 90%, at least91%, at least 92%, at least 93%, at least 94%, at least 95%, at least96%, at least 97%, at least 98% or at least 99% to the polypeptide ofSEQ ID NO: 15. In one embodiment, the polypeptides differ by up to 25amino acids, e.g., between 1 and 25 amino acids, such as 1-25, 1-20,1-15, 1-10 or 1-5 amino acids, or 1, 2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12,13, 14, 15, 16, 17, 18, 19, 20, 21, 22, 23, 24 or 25 amino acids fromSEQ ID NO: 15. In an embodiment, the animal feed or animal feed additivefurther comprises a formulating agent as described in the formulatingagent section above. In a further embodiment, the formulating agentcomprises one or more of the following compounds: glycerol, ethyleneglycol, 1,2-propylene glycol or 1,3-propylene glycol, sodium chloride,sodium benzoate, potassium sorbate, sodium sulfate, potassium sulfate,magnesium sulfate, sodium thiosulfate, calcium carbonate, sodiumcitrate, dextrin, glucose, sucrose, sorbitol, lactose, starch andcellulose. In an embodiment, the animal feed or animal feed additivecomprises one or more additional enzymes. In a preferred embodiment, theanimal feed or animal feed additive further comprises one or more GH10or GH11 polypeptides having xylanase activity. In an embodiment, theanimal feed or animal feed additive comprises one or more microbes. Inan embodiment, the animal feed or animal feed additive comprises one ormore vitamins. In an embodiment, the animal feed or animal feed additivecomprises one or more minerals. In an embodiment, the animal feed oranimal feed additive comprises one or more amino acids. In a furtherembodiment, the animal feed or animal feed additive further comprisesone or more formulating agents and one or more components selected fromthe list consisting of: one or more additional enzymes; one or moremicrobes; one or more vitamins; one or more minerals; one or more aminoacids; and one or more other feed ingredients.

In one embodiment, the animal feed or an animal feed additive comprisesa polypeptide comprising or consisting of the amino acid sequence of SEQID NO: 15 or an allelic variant thereof; or is a fragment thereof havingarabinofuranosidase activity and having at least 90% such as at least91%, at least 92%, at least 93%, at least 94%, at least 95%, at least96%, at least 97%, at least 98% or at least 99% of the length of thepolypeptide. In another embodiment, animal feed or an animal feedadditive comprises a polypeptide comprising or consisting of amino acids1 to 323 of SEQ ID NO: 15. In another embodiment, animal feed or ananimal feed additive comprises a polypeptide comprising or consisting ofamino acids 1 to 331 of SEQ ID NO: 180.

In another embodiment, the animal feed or an animal feed additivecomprises a variant polypeptide having arabinofuranosidase activitywherein the polypeptide is a variant of SEQ ID NO: 15 comprising one ormore amino acid substitutions, and/or one or more amino acid deletions,and/or one or more amino acid insertions or any combination thereof in1, 2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, 15, 16, 17, 18, 19, 20,21, 22, 23, 24 or 25 positions. In an embodiment, the number ofpositions comprising one or more amino acid substitutions, and/or one ormore amino acid deletions, and/or one or more amino acid insertions orany combination thereof in SEQ ID NO: 15 is not more than 10, e.g., 1,2, 3, 4, 5, 6, 7, 8, 9 or 10. In another embodiment, the number ofsubstitutions, deletions, and/or insertions in SEQ ID NO: 15 is not morethan 10, e.g., 1, 2, 3, 4, 5, 6, 7, 8, 9 or 10. In a further embodiment,the number of substitutions, preferably conservative substitutions, inSEQ ID NO: 15 is not more than 10, e.g., 1, 2, 3, 4, 5, 6, 7, 8, 9 or10. Examples of amino acid changes and conservative substitutions aredescribed in the second aspect of the invention.

The present invention also relates to an animal feed or an animal feedadditive comprising a polypeptide having arabinofuranosidase activityand having at least 80% sequence identity, e.g., at least 85%, at least86%, at least 87%, at least 88%, at least 89%, at least 90%, at least91%, at least 92%, at least 93%, at least 94%, at least 95%, at least96%, at least 97%, at least 98% or at least 99% to the polypeptide ofSEQ ID NO: 18. In one embodiment, the polypeptides differ by up to 25amino acids, e.g., between 1 and 25 amino acids, such as 1-25, 1-20,1-15, 1-10 or 1-5 amino acids, or 1, 2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12,13, 14, 15, 16, 17, 18, 19, 20, 21, 22, 23, 24 or 25 amino acids fromSEQ ID NO: 18. In an embodiment, the animal feed or animal feed additivefurther comprises a formulating agent as described in the formulatingagent section above. In a further embodiment, the formulating agentcomprises one or more of the following compounds: glycerol, ethyleneglycol, 1,2-propylene glycol or 1,3-propylene glycol, sodium chloride,sodium benzoate, potassium sorbate, sodium sulfate, potassium sulfate,magnesium sulfate, sodium thiosulfate, calcium carbonate, sodiumcitrate, dextrin, glucose, sucrose, sorbitol, lactose, starch andcellulose. In an embodiment, the animal feed or animal feed additivecomprises one or more additional enzymes. In a preferred embodiment, theanimal feed or animal feed additive further comprises one or more GH10or GH11 polypeptides having xylanase activity. In an embodiment, theanimal feed or animal feed additive comprises one or more microbes. Inan embodiment, the animal feed or animal feed additive comprises one ormore vitamins. In an embodiment, the animal feed or animal feed additivecomprises one or more minerals. In an embodiment, the animal feed oranimal feed additive comprises one or more amino acids. In a furtherembodiment, the animal feed or animal feed additive further comprisesone or more formulating agents and one or more components selected fromthe list consisting of: one or more additional enzymes; one or moremicrobes; one or more vitamins; one or more minerals; one or more aminoacids; and one or more other feed ingredients.

In one embodiment, the animal feed or an animal feed additive comprisesa polypeptide comprising or consisting of the amino acid sequence of SEQID NO: 18 or an allelic variant thereof; or is a fragment thereof havingarabinofuranosidase activity and having at least 90% such as at least91%, at least 92%, at least 93%, at least 94%, at least 95%, at least96%, at least 97%, at least 98% or at least 99% of the length of thepolypeptide. In another embodiment, animal feed or an animal feedadditive comprises a polypeptide comprising or consisting of amino acids1 to 323 of SEQ ID NO: 18. In another embodiment, animal feed or ananimal feed additive comprises a polypeptide comprising or consisting ofamino acids 1 to 331 of SEQ ID NO: 180.

In another embodiment, the animal feed or an animal feed additivecomprises a variant polypeptide having arabinofuranosidase activitywherein the polypeptide is a variant of SEQ ID NO: 18 comprising one ormore amino acid substitutions, and/or one or more amino acid deletions,and/or one or more amino acid insertions or any combination thereof in1, 2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, 15, 16, 17, 18, 19, 20,21, 22, 23, 24 or 25 positions. In an embodiment, the number ofpositions comprising one or more amino acid substitutions, and/or one ormore amino acid deletions, and/or one or more amino acid insertions orany combination thereof in SEQ ID NO: 18 is not more than 10, e.g., 1,2, 3, 4, 5, 6, 7, 8, 9 or 10. In another embodiment, the number ofsubstitutions, deletions, and/or insertions in SEQ ID NO: 18 is not morethan 10, e.g., 1, 2, 3, 4, 5, 6, 7, 8, 9 or 10. In a further embodiment,the number of substitutions, preferably conservative substitutions, inSEQ ID NO: 18 is not more than 10, e.g., 1, 2, 3, 4, 5, 6, 7, 8, 9 or10. Examples of amino acid changes and conservative substitutions aredescribed in the second aspect of the invention.

The present invention also relates to an animal feed or an animal feedadditive comprising a polypeptide having arabinofuranosidase activityand having at least 80% sequence identity, e.g., at least 85%, at least86%, at least 87%, at least 88%, at least 89%, at least 90%, at least91%, at least 92%, at least 93%, at least 94%, at least 95%, at least96%, at least 97%, at least 98% or at least 99% to the polypeptide ofSEQ ID NO: 21. In one embodiment, the polypeptides differ by up to 25amino acids, e.g., between 1 and 25 amino acids, such as 1-25, 1-20,1-15, 1-10 or 1-5 amino acids, or 1, 2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12,13, 14, 15, 16, 17, 18, 19, 20, 21, 22, 23, 24 or 25 amino acids fromSEQ ID NO: 21. In an embodiment, the animal feed or animal feed additivefurther comprises a formulating agent as described in the formulatingagent section above. In a further embodiment, the formulating agentcomprises one or more of the following compounds: glycerol, ethyleneglycol, 1,2-propylene glycol or 1,3-propylene glycol, sodium chloride,sodium benzoate, potassium sorbate, sodium sulfate, potassium sulfate,magnesium sulfate, sodium thiosulfate, calcium carbonate, sodiumcitrate, dextrin, glucose, sucrose, sorbitol, lactose, starch andcellulose. In an embodiment, the animal feed or animal feed additivecomprises one or more additional enzymes. In a preferred embodiment, theanimal feed or animal feed additive further comprises one or more GH10or GH11 polypeptides having xylanase activity. In an embodiment, theanimal feed or animal feed additive comprises one or more microbes. Inan embodiment, the animal feed or animal feed additive comprises one ormore vitamins. In an embodiment, the animal feed or animal feed additivecomprises one or more minerals. In an embodiment, the animal feed oranimal feed additive comprises one or more amino acids. In a furtherembodiment, the animal feed or animal feed additive further comprisesone or more formulating agents and one or more components selected fromthe list consisting of: one or more additional enzymes; one or moremicrobes; one or more vitamins; one or more minerals; one or more aminoacids; and one or more other feed ingredients.

In one embodiment, the animal feed or an animal feed additive comprisesa polypeptide comprising or consisting of the amino acid sequence of SEQID NO: 21 or an allelic variant thereof; or is a fragment thereof havingarabinofuranosidase activity and having at least 90% such as at least91%, at least 92%, at least 93%, at least 94%, at least 95%, at least96%, at least 97%, at least 98% or at least 99% of the length of thepolypeptide. In another embodiment, animal feed or an animal feedadditive comprises a polypeptide comprising or consisting of amino acids1 to 323 of SEQ ID NO: 21. In another embodiment, animal feed or ananimal feed additive comprises a polypeptide comprising or consisting ofamino acids 1 to 331 of SEQ ID NO: 180.

In another embodiment, the animal feed or an animal feed additivecomprises a variant polypeptide having arabinofuranosidase activitywherein the polypeptide is a variant of SEQ ID NO: 21 comprising one ormore amino acid substitutions, and/or one or more amino acid deletions,and/or one or more amino acid insertions or any combination thereof in1, 2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, 15, 16, 17, 18, 19, 20,21, 22, 23, 24 or 25 positions. In an embodiment, the number ofpositions comprising one or more amino acid substitutions, and/or one ormore amino acid deletions, and/or one or more amino acid insertions orany combination thereof in SEQ ID NO: 21 is not more than 10, e.g., 1,2, 3, 4, 5, 6, 7, 8, 9 or 10. In another embodiment, the number ofsubstitutions, deletions, and/or insertions in SEQ ID NO: 21 is not morethan 10, e.g., 1, 2, 3, 4, 5, 6, 7, 8, 9 or 10. In a further embodiment,the number of substitutions, preferably conservative substitutions, inSEQ ID NO: 21 is not more than 10, e.g., 1, 2, 3, 4, 5, 6, 7, 8, 9 or10. Examples of amino acid changes and conservative substitutions aredescribed in the second aspect of the invention.

The present invention also relates to an animal feed or an animal feedadditive comprising a polypeptide having arabinofuranosidase activityand having at least 80% sequence identity, e.g., at least 85%, at least86%, at least 87%, at least 88%, at least 89%, at least 90%, at least91%, at least 92%, at least 93%, at least 94%, at least 95%, at least96%, at least 97%, at least 98% or at least 99% to the polypeptide ofSEQ ID NO: 42. In one embodiment, the polypeptides differ by up to 25amino acids, e.g., between 1 and 25 amino acids, such as 1-25, 1-20,1-15, 1-10 or 1-5 amino acids, or 1, 2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12,13, 14, 15, 16, 17, 18, 19, 20, 21, 22, 23, 24 or 25 amino acids fromSEQ ID NO: 42. In an embodiment, the animal feed or animal feed additivefurther comprises a formulating agent as described in the formulatingagent section above. In a further embodiment, the formulating agentcomprises one or more of the following compounds: glycerol, ethyleneglycol, 1,2-propylene glycol or 1,3-propylene glycol, sodium chloride,sodium benzoate, potassium sorbate, sodium sulfate, potassium sulfate,magnesium sulfate, sodium thiosulfate, calcium carbonate, sodiumcitrate, dextrin, glucose, sucrose, sorbitol, lactose, starch andcellulose. In an embodiment, the animal feed or animal feed additivecomprises one or more additional enzymes. In a preferred embodiment, theanimal feed or animal feed additive further comprises one or more GH10or GH11 polypeptides having xylanase activity. In an embodiment, theanimal feed or animal feed additive comprises one or more microbes. Inan embodiment, the animal feed or animal feed additive comprises one ormore vitamins. In an embodiment, the animal feed or animal feed additivecomprises one or more minerals. In an embodiment, the animal feed oranimal feed additive comprises one or more amino acids. In a furtherembodiment, the animal feed or animal feed additive further comprisesone or more formulating agents and one or more components selected fromthe list consisting of: one or more additional enzymes; one or moremicrobes; one or more vitamins; one or more minerals; one or more aminoacids; and one or more other feed ingredients.

In one embodiment, the animal feed or an animal feed additive comprisesa polypeptide comprising or consisting of the amino acid sequence of SEQID NO: 42 or an allelic variant thereof; or is a fragment thereof havingarabinofuranosidase activity and having at least 90% such as at least91%, at least 92%, at least 93%, at least 94%, at least 95%, at least96%, at least 97%, at least 98% or at least 99% of the length of thepolypeptide. In another embodiment, animal feed or an animal feedadditive comprises a polypeptide comprising or consisting of amino acids1 to 323 of SEQ ID NO: 42. In another embodiment, animal feed or ananimal feed additive comprises a polypeptide comprising or consisting ofamino acids 1 to 331 of SEQ ID NO: 180.

In another embodiment, the animal feed or an animal feed additivecomprises a variant polypeptide having arabinofuranosidase activitywherein the polypeptide is a variant of SEQ ID NO: 42 comprising one ormore amino acid substitutions, and/or one or more amino acid deletions,and/or one or more amino acid insertions or any combination thereof in1, 2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, 15, 16, 17, 18, 19, 20,21, 22, 23, 24 or 25 positions. In an embodiment, the number ofpositions comprising one or more amino acid substitutions, and/or one ormore amino acid deletions, and/or one or more amino acid insertions orany combination thereof in SEQ ID NO: 42 is not more than 10, e.g., 1,2, 3, 4, 5, 6, 7, 8, 9 or 10. In another embodiment, the number ofsubstitutions, deletions, and/or insertions in SEQ ID NO: 42 is not morethan 10, e.g., 1, 2, 3, 4, 5, 6, 7, 8, 9 or 10. In a further embodiment,the number of substitutions, preferably conservative substitutions, inSEQ ID NO: 42 is not more than 10, e.g., 1, 2, 3, 4, 5, 6, 7, 8, 9 or10. Examples of amino acid changes and conservative substitutions aredescribed in the second aspect of the invention.

The present invention also relates to an animal feed or an animal feedadditive comprising a polypeptide having arabinofuranosidase activityand having at least 80% sequence identity, e.g., at least 85%, at least86%, at least 87%, at least 88%, at least 89%, at least 90%, at least91%, at least 92%, at least 93%, at least 94%, at least 95%, at least96%, at least 97%, at least 98% or at least 99% to the polypeptide ofSEQ ID NO: 132. In one embodiment, the polypeptides differ by up to 25amino acids, e.g., between 1 and 25 amino acids, such as 1-25, 1-20,1-15, 1-10 or 1-5 amino acids, or 1, 2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12,13, 14, 15, 16, 17, 18, 19, 20, 21, 22, 23, 24 or 25 amino acids fromSEQ ID NO: 132. In an embodiment, the animal feed or animal feedadditive further comprises a formulating agent as described in theformulating agent section above. In a further embodiment, theformulating agent comprises one or more of the following compounds:glycerol, ethylene glycol, 1,2-propylene glycol or 1,3-propylene glycol,sodium chloride, sodium benzoate, potassium sorbate, sodium sulfate,potassium sulfate, magnesium sulfate, sodium thiosulfate, calciumcarbonate, sodium citrate, dextrin, glucose, sucrose, sorbitol, lactose,starch and cellulose. In an embodiment, the animal feed or animal feedadditive comprises one or more additional enzymes. In a preferredembodiment, the animal feed or animal feed additive further comprisesone or more GH10 or GH11 polypeptides having xylanase activity. In anembodiment, the animal feed or animal feed additive comprises one ormore microbes. In an embodiment, the animal feed or animal feed additivecomprises one or more vitamins. In an embodiment, the animal feed oranimal feed additive comprises one or more minerals. In an embodiment,the animal feed or animal feed additive comprises one or more aminoacids. In a further embodiment, the animal feed or animal feed additivefurther comprises one or more formulating agents and one or morecomponents selected from the list consisting of: one or more additionalenzymes; one or more microbes; one or more vitamins; one or moreminerals; one or more amino acids; and one or more other feedingredients.

In one embodiment, the animal feed or an animal feed additive comprisesa polypeptide comprising or consisting of the amino acid sequence of SEQID NO: 132 or an allelic variant thereof; or is a fragment thereofhaving arabinofuranosidase activity and having at least 90% such as atleast 91%, at least 92%, at least 93%, at least 94%, at least 95%, atleast 96%, at least 97%, at least 98% or at least 99% of the length ofthe polypeptide. In another embodiment, animal feed or an animal feedadditive comprises a polypeptide comprising or consisting of amino acids1 to 323 of SEQ ID NO: 132. In another embodiment, animal feed or ananimal feed additive comprises a polypeptide comprising or consisting ofamino acids 1 to 331 of SEQ ID NO: 180.

In another embodiment, the animal feed or an animal feed additivecomprises a variant polypeptide having arabinofuranosidase activitywherein the polypeptide is a variant of SEQ ID NO: 132 comprising one ormore amino acid substitutions, and/or one or more amino acid deletions,and/or one or more amino acid insertions or any combination thereof in1, 2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, 15, 16, 17, 18, 19, 20,21, 22, 23, 24 or 25 positions. In an embodiment, the number ofpositions comprising one or more amino acid substitutions, and/or one ormore amino acid deletions, and/or one or more amino acid insertions orany combination thereof in SEQ ID NO: 132 is not more than 10, e.g., 1,2, 3, 4, 5, 6, 7, 8, 9 or 10. In another embodiment, the number ofsubstitutions, deletions, and/or insertions in SEQ ID NO: 132 is notmore than 10, e.g., 1, 2, 3, 4, 5, 6, 7, 8, 9 or 10. In a furtherembodiment, the number of substitutions, preferably conservativesubstitutions, in SEQ ID NO: 132 is not more than 10, e.g., 1, 2, 3, 4,5, 6, 7, 8, 9 or 10. Examples of amino acid changes and conservativesubstitutions are described in the second aspect of the invention.

The present invention also relates to an animal feed or an animal feedadditive comprising a polypeptide having arabinofuranosidase activityand having at least 80% sequence identity, e.g., at least 85%, at least86%, at least 87%, at least 88%, at least 89%, at least 90%, at least91%, at least 92%, at least 93%, at least 94%, at least 95%, at least96%, at least 97%, at least 98% or at least 99% to the polypeptide ofSEQ ID NO: 150. In one embodiment, the polypeptides differ by up to 25amino acids, e.g., between 1 and 25 amino acids, such as 1-25, 1-20,1-15, 1-10 or 1-5 amino acids, or 1, 2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12,13, 14, 15, 16, 17, 18, 19, 20, 21, 22, 23, 24 or 25 amino acids fromSEQ ID NO: 150. In an embodiment, the animal feed or animal feedadditive further comprises a formulating agent as described in theformulating agent section above. In a further embodiment, theformulating agent comprises one or more of the following compounds:glycerol, ethylene glycol, 1,2-propylene glycol or 1,3-propylene glycol,sodium chloride, sodium benzoate, potassium sorbate, sodium sulfate,potassium sulfate, magnesium sulfate, sodium thiosulfate, calciumcarbonate, sodium citrate, dextrin, glucose, sucrose, sorbitol, lactose,starch and cellulose. In an embodiment, the animal feed or animal feedadditive comprises one or more additional enzymes. In a preferredembodiment, the animal feed or animal feed additive further comprisesone or more GH10 or GH11 polypeptides having xylanase activity. In anembodiment, the animal feed or animal feed additive comprises one ormore microbes. In an embodiment, the animal feed or animal feed additivecomprises one or more vitamins. In an embodiment, the animal feed oranimal feed additive comprises one or more minerals. In an embodiment,the animal feed or animal feed additive comprises one or more aminoacids. In a further embodiment, the animal feed or animal feed additivefurther comprises one or more formulating agents and one or morecomponents selected from the list consisting of: one or more additionalenzymes; one or more microbes; one or more vitamins; one or moreminerals; one or more amino acids; and one or more other feedingredients.

In one embodiment, the animal feed or an animal feed additive comprisesa polypeptide comprising or consisting of the amino acid sequence of SEQID NO: 150 or an allelic variant thereof; or is a fragment thereofhaving arabinofuranosidase activity and having at least 90% such as atleast 91%, at least 92%, at least 93%, at least 94%, at least 95%, atleast 96%, at least 97%, at least 98% or at least 99% of the length ofthe polypeptide. In another embodiment, animal feed or an animal feedadditive comprises a polypeptide comprising or consisting of amino acids1 to 323 of SEQ ID NO: 150. In another embodiment, animal feed or ananimal feed additive comprises a polypeptide comprising or consisting ofamino acids 1 to 331 of SEQ ID NO: 180.

In another embodiment, the animal feed or an animal feed additivecomprises a variant polypeptide having arabinofuranosidase activitywherein the polypeptide is a variant of SEQ ID NO: 150 comprising one ormore amino acid substitutions, and/or one or more amino acid deletions,and/or one or more amino acid insertions or any combination thereof in1, 2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, 15, 16, 17, 18, 19, 20,21, 22, 23, 24 or 25 positions. In an embodiment, the number ofpositions comprising one or more amino acid substitutions, and/or one ormore amino acid deletions, and/or one or more amino acid insertions orany combination thereof in SEQ ID NO: 150 is not more than 10, e.g., 1,2, 3, 4, 5, 6, 7, 8, 9 or 10. In another embodiment, the number ofsubstitutions, deletions, and/or insertions in SEQ ID NO: 150 is notmore than 10, e.g., 1, 2, 3, 4, 5, 6, 7, 8, 9 or 10. In a furtherembodiment, the number of substitutions, preferably conservativesubstitutions, in SEQ ID NO: 150 is not more than 10, e.g., 1, 2, 3, 4,5, 6, 7, 8, 9 or 10. Examples of amino acid changes and conservativesubstitutions are described in the second aspect of the invention.

The present invention also relates to an animal feed or an animal feedadditive comprising a polypeptide having arabinofuranosidase activityand having at least 80% sequence identity, e.g., at least 85%, at least86%, at least 87%, at least 88%, at least 89%, at least 90%, at least91%, at least 92%, at least 93%, at least 94%, at least 95%, at least96%, at least 97%, at least 98% or at least 99% to the polypeptide ofSEQ ID NO: 159. In one embodiment, the polypeptides differ by up to 25amino acids, e.g., between 1 and 25 amino acids, such as 1-25, 1-20,1-15, 1-10 or 1-5 amino acids, or 1, 2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12,13, 14, 15, 16, 17, 18, 19, 20, 21, 22, 23, 24 or 25 amino acids fromSEQ ID NO: 159. In an embodiment, the animal feed or animal feedadditive further comprises a formulating agent as described in theformulating agent section above. In a further embodiment, theformulating agent comprises one or more of the following compounds:glycerol, ethylene glycol, 1,2-propylene glycol or 1,3-propylene glycol,sodium chloride, sodium benzoate, potassium sorbate, sodium sulfate,potassium sulfate, magnesium sulfate, sodium thiosulfate, calciumcarbonate, sodium citrate, dextrin, glucose, sucrose, sorbitol, lactose,starch and cellulose. In an embodiment, the animal feed or animal feedadditive comprises one or more additional enzymes. In a preferredembodiment, the animal feed or animal feed additive further comprisesone or more GH10 or GH11 polypeptides having xylanase activity. In anembodiment, the animal feed or animal feed additive comprises one ormore microbes. In an embodiment, the animal feed or animal feed additivecomprises one or more vitamins. In an embodiment, the animal feed oranimal feed additive comprises one or more minerals. In an embodiment,the animal feed or animal feed additive comprises one or more aminoacids. In a further embodiment, the animal feed or animal feed additivefurther comprises one or more formulating agents and one or morecomponents selected from the list consisting of: one or more additionalenzymes; one or more microbes; one or more vitamins; one or moreminerals; one or more amino acids; and one or more other feedingredients.

In one embodiment, the animal feed or an animal feed additive comprisesa polypeptide comprising or consisting of the amino acid sequence of SEQID NO: 159 or an allelic variant thereof; or is a fragment thereofhaving arabinofuranosidase activity and having at least 90% such as atleast 91%, at least 92%, at least 93%, at least 94%, at least 95%, atleast 96%, at least 97%, at least 98% or at least 99% of the length ofthe polypeptide. In another embodiment, animal feed or an animal feedadditive comprises a polypeptide comprising or consisting of amino acids1 to 323 of SEQ ID NO: 159. In another embodiment, animal feed or ananimal feed additive comprises a polypeptide comprising or consisting ofamino acids 1 to 331 of SEQ ID NO: 180.

In another embodiment, the animal feed or an animal feed additivecomprises a variant polypeptide having arabinofuranosidase activitywherein the polypeptide is a variant of SEQ ID NO: 159 comprising one ormore amino acid substitutions, and/or one or more amino acid deletions,and/or one or more amino acid insertions or any combination thereof in1, 2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, 15, 16, 17, 18, 19, 20,21, 22, 23, 24 or 25 positions. In an embodiment, the number ofpositions comprising one or more amino acid substitutions, and/or one ormore amino acid deletions, and/or one or more amino acid insertions orany combination thereof in SEQ ID NO: 159 is not more than 10, e.g., 1,2, 3, 4, 5, 6, 7, 8, 9 or 10. In another embodiment, the number ofsubstitutions, deletions, and/or insertions in SEQ ID NO: 159 is notmore than 10, e.g., 1, 2, 3, 4, 5, 6, 7, 8, 9 or 10. In a furtherembodiment, the number of substitutions, preferably conservativesubstitutions, in SEQ ID NO: 159 is not more than 10, e.g., 1, 2, 3, 4,5, 6, 7, 8, 9 or 10. Examples of amino acid changes and conservativesubstitutions are described in the second aspect of the invention.

Animal feed compositions or diets have a relatively high content ofprotein. Poultry and pig diets can be characterised as indicated inTable B of WO 01/58275, columns 2-3. Fish diets can be characterised asindicated in column 4 of this Table B. Furthermore such fish dietsusually have a crude fat content of 200-310 g/kg.

An animal feed composition according to the invention has a crudeprotein content of 50-800 g/kg, and furthermore comprises at least onexylanase as claimed herein and/or at least one arabinofuranosidase asclaimed herein.

Furthermore, or in the alternative (to the crude protein contentindicated above), the animal feed composition of the invention has acontent of metabolisable energy of 10-30 MJ/kg; and/or a content ofcalcium of 0.1-200 g/kg; and/or a content of available phosphorus of0.1-200 g/kg; and/or a content of methionine of 0.1-100 g/kg; and/or acontent of methionine plus cysteine of 0.1-150 g/kg; and/or a content oflysine of 0.5-50 g/kg.

In particular embodiments, the content of metabolisable energy, crudeprotein, calcium, phosphorus, methionine, methionine plus cysteine,and/or lysine is within any one of ranges 2, 3, 4 or 5 in Table B of WO01/58275 (R. 2-5).

Crude protein is calculated as nitrogen (N) multiplied by a factor 6.25,i.e. Crude protein (g/kg)=N (g/kg)×6.25. The nitrogen content isdetermined by the Kjeldahl method (A.O.A.C., 1984, Official Methods ofAnalysis 14th ed., Association of Official Analytical Chemists,Washington D.C.).

Metabolisable energy can be calculated on the basis of the NRCpublication Nutrient requirements in swine, tenth revised edition 1988,subcommittee on swine nutrition, committee on animal nutrition, board ofagriculture, national research council. National Academy Press,Washington, D.C., pp. 2-6, and the European Table of Energy Values forPoultry Feed-stuffs, Spelderholt centre for poultry research andextension, 7361 D A Beekbergen, The Netherlands. Grafisch bedrijf Ponsen& Iooijen by, Wageningen. ISBN 90-71463-12-5.

The dietary content of calcium, available phosphorus and amino acids incomplete animal diets is calculated on the basis of feed tables such asVeevoedertabel 1997, gegevens over chemische samenstelling,verteerbaarheid en voederwaarde van voedermiddelen, CentralVeevoederbureau, Runderweg 6, 8219 pk Lelystad. ISBN 90-72839-13-7.

In a particular embodiment, the animal feed composition of the inventioncontains at least one vegetable protein as defined above.

The animal feed composition of the invention may also contain animalprotein, such as Meat and Bone Meal, Feather meal, and/or Fish Meal,typically in an amount of 0-25%. The animal feed composition of theinvention may also comprise Dried Distillers Grains with Solubles(DDGS), typically in amounts of 0-30%.

In still further particular embodiments, the animal feed composition ofthe invention contains 0-80% maize; and/or 0-80% sorghum; and/or 0-70%wheat; and/or 0-70% Barley; and/or 0-30% oats; and/or 0-40% soybeanmeal; and/or 0-25% fish meal; and/or 0-25% meat and bone meal; and/or0-20% whey.

The animal feed may comprise vegetable proteins. In particularembodiments, the protein content of the vegetable proteins is at least10, 20, 30, 40, 50, 60, 70, 80, or 90% (w/w). Vegetable proteins may bederived from vegetable protein sources, such as legumes and cereals, forexample, materials from plants of the families Fabaceae (Leguminosae),Cruciferaceae, Chenopodiaceae, and Poaceae, such as soy bean meal, lupinmeal, rapeseed meal, and combinations thereof.

In a particular embodiment, the vegetable protein source is materialfrom one or more plants of the family Fabaceae, e.g., soybean, lupine,pea, or bean. In another particular embodiment, the vegetable proteinsource is material from one or more plants of the family Chenopodiaceae,e.g. beet, sugar beet, spinach or quinoa. Other examples of vegetableprotein sources are rapeseed, and cabbage. In another particularembodiment, soybean is a preferred vegetable protein source. Otherexamples of vegetable protein sources are cereals such as barley, wheat,rye, oat, maize (corn), rice, and sorghum.

Animal diets can e.g. be manufactured as mash feed (non-pelleted) orpelleted feed. Typically, the milled feed-stuffs are mixed andsufficient amounts of essential vitamins and minerals are addedaccording to the specifications for the species in question. Enzymes canbe added as solid or liquid enzyme formulations. For example, for mashfeed a solid or liquid enzyme formulation may be added before or duringthe ingredient mixing step. For pelleted feed the (liquid or solid)xylanase/enzyme preparation may also be added before or during the feedingredient step. Typically a liquid enzyme preparation comprises thexylanase and/or arabinofuranosidase of the invention optionally with apolyol, such as glycerol, ethylene glycol or propylene glycol, and isadded after the pelleting step, such as by spraying the liquidformulation onto the pellets. The enzyme may also be incorporated in afeed additive or premix.

Alternatively, the xylanase and/or arabinofuranosidase can be preparedby freezing a mixture of liquid enzyme solution with a bulking agentsuch as ground soybean meal, and then lyophilizing the mixture.

The final enzyme concentration in the diet is within the range of0.01-200 mg enzyme protein per kg diet, preferably between 0.05-100mg/kg, more preferably 0.1-50 mg/kg, even more preferably 0.2-20 mgenzyme protein per kg animal diet, for each enzyme.

It is at present contemplated that the xylanase is administered in oneor more of the following amounts (dosage ranges): 0.01-200; 0.05-100;0.1-50; 0.2-20; 0.1-1; 0.2-2; 0.5-5; or 1-10 wherein all these rangesare mg xylanase protein per kg feed (ppm). It is at present contemplatedthat the arabinofuranosidase is administered in one or more of thefollowing amounts (dosage ranges): 0.01-200; 0.05-100; 0.1-50; 0.2-20;0.1-1; 0.2-2; 0.5-5; or 1-10 wherein all these ranges are mgarabinofuranosidase protein per kg feed (ppm). It is furthercontemplated that the ratio of the GH10 or 11 xylanase to GH62arabinofuranosidase is in the range of 100:1 to 1:100 xylanase:arabinofuranosidase such as the ranges 50:1 to 1:50, 50:1 to 1:10, 25:1to 1:5, 10:1 to 1:2 or such as 10:1 to 1:50, 5:1 to 1:25, 2:1 to 1:10xylanase:arabinofuranosidase.

For determining mg xylanase and/or mg arabinofuranosidase protein per kgfeed, the xylanase and/or arabinofuranosidase is purified from the feedcomposition, and the specific activity of the purified xylanase and/orarabinofuranosidase is determined using a relevant assay (see underxylanase or arabinofuranosidase activity). The xylanase and/orarabinofuranosidase activity of the feed composition as such is alsodetermined using the same assay, and on the basis of these twodeterminations, the dosage in mg xylanase and/or mg arabinofuranosidaseprotein per kg feed is calculated.

In a particular embodiment, the animal feed additive of the invention isintended for being included (or prescribed as having to be included) inanimal diets or feed at levels of 0.01 to 10.0%; more particularly 0.05to 5.0%; or 0.2 to 1.0% (% meaning g additive per 100 g feed). This isso in particular for premixes.

The same principles apply for determining mg xylanase or mgarabinofuranosidase protein in feed additives. Of course, if a sample isavailable of the xylanase or arabinofuranosidase used for preparing thefeed additive or the feed, the specific activity is determined from thissample (no need to purify the xylanase or arabinofuranosidase from thefeed composition or the additive).

Additional Enzymes

In another embodiment, the compositions described herein optionallyinclude one or more enzymes. Enzymes can be classified on the basis ofthe handbook Enzyme Nomenclature from NC-IUBMB, 1992), see also theENZYME site at the internet: http://www.expasy.ch/enzyme/. ENZYME is arepository of information relative to the nomenclature of enzymes. It isprimarily based on the recommendations of the Nomenclature Committee ofthe International Union of Biochemistry and Molecular Biology (IUB-MB),Academic Press, Inc., 1992, and it describes each type of characterizedenzyme for which an EC (Enzyme Commission) number has been provided(Bairoch A. The ENZYME database, 2000, Nucleic Acids Res 28:304-305).This IUB-MB Enzyme nomenclature is based on their substrate specificityand occasionally on their molecular mechanism; such a classificationdoes not reflect the structural features of these enzymes.

Another classification of certain glycoside hydrolase enzymes, such asendoglucanase, xylanase, galactanase, mannanase, dextranase, lysozymeand galactosidase is described in Henrissat et al, “Thecarbohydrate-active enzymes database (CAZy) in 2013”, Nucl. Acids Res.(1 Jan. 2014) 42 (D1): D490-D495; see also www.cazy.org.

Thus the composition of the invention may also comprise at least oneother enzyme selected from the group comprising of phytase (EC 3.1.3.8or 3.1.3.26); xylanase (EC 3.2.1.8); galactanase (EC 3.2.1.89);alpha-galactosidase (EC 3.2.1.22); protease (EC 3.4); phospholipase A1(EC 3.1.1.32); phospholipase A2 (EC 3.1.1.4); lysophospholipase (EC3.1.1.5); phospholipase C (3.1.4.3); phospholipase D (EC 3.1.4.4);amylase such as, for example, alpha-amylase (EC 3.2.1.1); lysozyme (EC3.2.1.17); arabinofuranosidase (EC 3.2.1.55); beta-xylosidase (EC3.2.1.37); acetyl xylan esterase (EC 3.1.1.72); feruloyl esterase (EC3.1.1.73); cellulase (EC 3.2.1.4); cellobiohydrolases (EC 3.2.1.91);beta-glucosidase (EC 3.2.1.21); pullulanase (EC 3.2.1.41) andbeta-glucanase (EC 3.2.1.4 or EC 3.2.1.6), or any mixture thereof.

In a particular embodiment, the composition of the invention comprises aphytase (EC 3.1.3.8 or 3.1.3.26). Examples of commercially availablephytases include Bio-Feed™ Phytase (Novozymes), Ronozyme® P, Ronozyme®NP and Ronozyme® HiPhos (DSM Nutritional Products), Natuphos™ (BASF),Finase® and Quantum® Blue (AB Enzymes), OptiPhos® (Huvepharma) Phyzyme®XP (Verenium/DuPont) and Axtra® PHY (DuPont). Other preferred phytasesinclude those described in e.g. WO 98/28408, WO 00/43503, and WO03/066847.

In a particular embodiment, the composition of the invention comprises axylanase (EC 3.2.1.8). Examples of commercially available xylanasesinclude Ronozyme® WX and Ronozyme® G2 (DSM Nutritional Products),Econase® XT and Barley (AB Vista), Xylathin® (Verenium), Hostazym® X(Huvepharma) and Axtra® XB (Xylanase/beta-glucanase, DuPont)

In a particular embodiment, the composition of the invention comprises aprotease (EC 3.4). Examples of commercially available proteases includeRonozyme® ProAct (DSM Nutritional Products).

Microbes

In an embodiment, the animal feed composition further comprises one ormore additional microbes. In a particular embodiment, the animal feedcomposition further comprises a bacterium from one or more of thefollowing genera: Lactobacillus, Lactococcus, Streptococcus, Bacillus,Pediococcus, Enterococcus, Leuconostoc, Carnobacterium,Propionibacterium, Bifidobacterium, Clostridium and Megasphaera or anycombination thereof.

In a preferred embodiment, animal feed composition further comprises abacterium from one or more of the following strains: Bacillus subtilis,Bacillus licheniformis, Bacillus amyloliquefaciens, Bacillus cereus,Bacillus pumilus, Bacillus polymyxa, Bacillus megaterium, Bacilluscoagulans, Bacillus circulans, Bifidobacterium bifidum, Bifidobacteriumanimalis, Bifidobacterium sp., Carnobacterium sp., Clostridiumbutyricum, Clostridium sp., Enterococcus faecium, Enterococcus sp.,Lactobacillus sp., Lactobacillus acidophilus, Lactobacillus farciminus,Lactobacillus rhamnosus, Lactobacillus reuteri, Lactobacillussalivarius, Lactococcus lactis, Lactococcus sp., Leuconostoc sp.,Megasphaera elsdenii, Megasphaera sp., Pediococsus acidilactici,Pediococcus sp., Propionibacterium thoenii, Propionibacterium sp. andStreptococcus sp.

In a more preferred embodiment, animal feed composition furthercomprises a bacterium from one or more of the following strains ofBacillus subtilis: 3A-P4 (PTA-6506); 15A-P4 (PTA-6507); 22C-P1(PTA-6508); 2084 (NRRL B-500130); LSSA01 (NRRL-B-50104); BS27 (NRRLB-501 05); BS 18 (NRRL B-50633); and BS 278 (NRRL B-50634).

The bacterial count of each of the bacterial strains in the animal feedcomposition is between 1×10⁴ and 1×10¹⁴ CFU/kg of dry matter, preferablybetween 1×10⁶ and 1×10¹² CFU/kg of dry matter, and more preferablybetween 1×10⁷ and 1×10¹¹ CFU/kg of dry matter. In a more preferredembodiment the bacterial count of each of the bacterial strains in theanimal feed composition is between 1×10⁸ and 1×10¹⁰ CFU/kg of drymatter.

The bacterial count of each of the bacterial strains in the animal feedcomposition is between 1×10⁵ and 1×10¹⁵ CFU/animal/day, preferablybetween 1×10⁷ and 1×10¹³ CFU/animal/day, and more preferably between1×10⁸ and 1×10¹² CFU/animal/day. In a more preferred embodiment thebacterial count of each of the bacterial strains in the animal feedcomposition is between 1×10⁹ and 1×10¹¹ CFU/animal/day.

In another embodiment, the one or more bacterial strains are present inthe form of a stable spore.

Premix

In an embodiment, the animal feed may include a premix, comprising e.g.vitamins, minerals, enzymes, preservatives, antibiotics, other feedingredients or any combination thereof which are mixed into the animalfeed.

Vitamins and Minerals

In another embodiment, the animal feed may include one or more vitamins,such as one or more fat-soluble vitamins and/or one or morewater-soluble vitamins. In another embodiment, the animal feed mayoptionally include one or more minerals, such as one or more traceminerals and/or one or more macro minerals.

Usually fat- and water-soluble vitamins, as well as trace minerals formpart of a so-called premix intended for addition to the feed, whereasmacro minerals are usually separately added to the feed.

Non-limiting examples of fat-soluble vitamins include vitamin A, vitaminD3, vitamin E, and vitamin K, e.g., vitamin K3.

Non-limiting examples of water-soluble vitamins include vitamin B12,biotin and choline, vitamin B1, vitamin B2, vitamin B6, niacin, folicacid and panthothenate, e.g., Ca-D-panthothenate.

Non-limiting examples of trace minerals include boron, cobalt, chloride,chromium, copper, fluoride, iodine, iron, manganese, molybdenum,selenium and zinc.

Non-limiting examples of macro minerals include calcium, magnesium,potassium and sodium.

The nutritional requirements of these components (exemplified withpoultry and piglets/pigs) are listed in Table A of WO 01/58275.Nutritional requirement means that these components should be providedin the diet in the concentrations indicated.

In the alternative, the animal feed additive of the invention comprisesat least one of the individual components specified in Table A of WO01/58275. At least one means either of, one or more of, one, or two, orthree, or four and so forth up to all thirteen, or up to all fifteenindividual components. More specifically, this at least one individualcomponent is included in the additive of the invention in such an amountas to provide an in-feed-concentration within the range indicated incolumn four, or column five, or column six of Table A.

In a still further embodiment, the animal feed additive of the inventioncomprises at least one of the below vitamins, preferably to provide anin-feed-concentration within the ranges specified in the below Table 1(for piglet diets, and broiler diets, respectively).

TABLE 1 Typical vitamin recommendations Vitamin Piglet diet Broiler dietVitamin A 10,000-15,000 IU/kg feed 8-12,500 IU/kg feed Vitamin D31800-2000 IU/kg feed 3000-5000 IU/kg feed Vitamin E 60-100 mg/kg feed150-240 mg/kg feed Vitamin K3 2-4 mg/kg feed 2-4 mg/kg feed Vitamin B12-4 mg/kg feed 2-3 mg/kg feed Vitamin B2 6-10 mg/kg feed 7-9 mg/kg feedVitamin B6 4-8 mg/kg feed 3-6 mg/kg feed Vitamin B12 0.03-0.05 mg/kgfeed 0.015-0.04 mg/kg feed Niacin 30-50 mg/kg feed 50-80 mg/kg feed(Vitamin B3) Pantothenic 20-40 mg/kg feed 10-18 mg/kg feed acid Folicacid 1-2 mg/kg feed 1-2 mg/kg feed Biotin 0.15-0.4 mg/kg feed 0.15-0.3mg/kg feed Choline 200-400 mg/kg feed 300-600 mg/kg feed chlorideAmino Acids

The composition of the invention may further comprise one or more aminoacids. Examples of amino acids which are used in animal feed are lysine,alanine, beta-alanine, threonine, methionine and tryptophan.

Other Feed Ingredients

The composition of the invention may further comprise colouring agents,stabilisers, growth improving additives and aroma compounds/flavourings,polyunsaturated fatty acids (PUFAs); reactive oxygen generating species,anti-microbial peptides and anti-fungal polypeptides.

Examples of colouring agents are carotenoids such as beta-carotene,astaxanthin, and lutein.

Examples of aroma compounds/flavourings are creosol, anethol, deca-,undeca- and/or dodeca-lactones, ionones, irone, gingerol, piperidine,propylidene phatalide, butylidene phatalide, capsaicin and tannin.

Examples of antimicrobial peptides (AMP's) are CAP18, Leucocin A,Tritrpticin, Protegrin-1, Thanatin, Defensin, Lactoferrin,Lactoferricin, and Ovispirin such as Novispirin (Robert Lehrer, 2000),Plectasins, and Statins, including the compounds and polypeptidesdisclosed in WO 03/044049 and WO 03/048148, as well as variants orfragments of the above that retain antimicrobial activity.

Examples of antifungal polypeptides (AFP's) are the Aspergillusgiganteus, and Aspergillus niger peptides, as well as variants andfragments thereof which retain antifungal activity, as disclosed in WO94/01459 and WO 02/090384.

Examples of polyunsaturated fatty acids are C18, C20 and C22polyunsaturated fatty acids, such as arachidonic acid, docosohexaenoicacid, eicosapentaenoic acid and gamma-linoleic acid.

Examples of reactive oxygen generating species are chemicals such asperborate, persulphate, or percarbonate; and enzymes such as an oxidase,an oxygenase or a syntethase.

The composition of the invention may further comprise at least one aminoacid. Examples of amino acids which are used in animal feed are lysine,alanine, beta-alanine, threonine, methionine and tryptophan.

Uses

The present invention is also directed to methods for using thepolypeptides having xylanase and/or arabinofuranosidase activity, orcompositions thereof, for e.g. animal feed. The present invention isalso directed to processes for using the polypeptides having xylanaseand/or arabinofuranosidase activity, or compositions thereof, such ase.g. those described below.

Use in Animal Feed

The present invention is also directed to methods for using thexylanases and/or arabinofuranosidase of the invention in animal feed.

The term animal includes all animals. Examples of animals arenon-ruminants, and ruminants. Ruminant animals include, for example,animals such as sheep, goats, and cattle, e.g. beef cattle, cows, andyoung calves. In a particular embodiment, the animal is a non-ruminantanimal. Non-ruminant animals include mono-gastric animals, e.g. pigs orswine (including, but not limited to, piglets, growing pigs, and sows);poultry such as turkeys, ducks and chicken (including but not limited tobroiler chicks, layers); horses (including but not limited to hotbloods,coldbloods and warm bloods), young calves; and fish (including but notlimited to salmon, trout, tilapia, catfish and carps; and crustaceans(including but not limited to shrimps and prawns).

In the use according to the invention the xylanases and/orarabinofuranosidases can be fed to the animal before, after, orsimultaneously with the diet. The latter is preferred.

In a particular embodiment, the form in which the xylanase and/orarabinofuranosidase is added to the feed, or animal feed additive, iswell-defined. Well-defined means that the xylanase and/orarabinofuranosidase preparation is at least 50% pure as determined bySize-exclusion chromatography (see Example 12 of WO 01/58275). In otherparticular embodiments the xylanase and/or arabinofuranosidasepreparation is at least 60, 70, 80, 85, 88, 90, 92, 94, or at least 95%pure as determined by this method.

A well-defined xylanase and/or arabinofuranosidase preparation isadvantageous. For instance, it is much easier to dose correctly to thefeed a xylanase and/or arabinofuranosidase that is essentially free frominterfering or contaminating other xylanases and/orarabinofuranosidases. The term dose correctly refers in particular tothe objective of obtaining consistent and constant results, and thecapability of optimizing dosage based upon the desired effect.

For the use in animal feed, however, the xylanase and/orarabinofuranosidase need not be that pure; it may e.g. include otherenzymes, in which case it could be termed a xylanase and/orarabinofuranosidase preparation.

The xylanase and/or arabinofuranosidase preparation can be (a) addeddirectly to the feed, or (b) it can be used in the production of one ormore intermediate compositions such as feed additives or premixes thatis subsequently added to the feed (or used in a treatment process). Thedegree of purity described above refers to the purity of the originalxylanase and/or arabinofuranosidase preparation, whether used accordingto (a) or (b) above.

Preferred Embodiments of the Invention

Preferred embodiments of the invention are described in the set of itemsbelow.

-   1. A composition comprising one or more GH10 or GH11 polypeptides    having xylanase activity and one or more GH62 polypeptides having    arabinofuranosidase activity, wherein:    -   (a) the GH62 polypeptide comprises the motif        [H/Y][L/M]F[F/S][A/C/H/S/T/V][A/D/G/N/R]D[D/E/N]G (SEQ ID NO:        1);    -   (b) the GH10 or GH11 polypeptide and the GH62 polypeptide        together solubilise at least 2.0% xylose from defatted        destarched maize (DFDSM); and    -   (c) the GH10 or GH11 polypeptide and the GH62 polypeptide        together solubilise at least 2 times more xylose from DFDSM than        the GH10 or GH11 polypeptide can when the GH62 polypeptide is        not present;    -   wherein (b) and (c) are performed under the reaction conditions:        -   i) 25 mg GH10 or GH11 polypeptide per kg DFDSM,        -   ii) 12.5 mg GH62 polypeptide per kg DFDSM, and        -   iii) incubation at 40° C., pH 5 for 4 hours.-   2. The composition of item 1, wherein the GH62 polypeptide comprises    one or more motifs selected from the list consisting of    [H/Y]LF[F/S][A/S/V][A/D/G]DNG (SEQ ID NO: 2), YLFF[A/V][A/G]DNG (SEQ    ID NO: 3), YLFFAGDNG (SEQ ID NO: 4), [H/Y]LFSSDDNG (SEQ ID NO: 5),    and YLFSSDDNG (SEQ ID NO: 6).-   3. The composition of any of items 1 to 2, wherein the GH62    polypeptide having arabinofuranosidase activity is selected from the    group consisting of:    -   (a) a polypeptide having at least 80% sequence identity to the        polypeptide of SEQ ID NO: 9;    -   (b) a polypeptide having at least 80% sequence identity to the        polypeptide of SEQ ID NO: 12;    -   (c) a polypeptide having at least 80% sequence identity to the        polypeptide of SEQ ID NO: 15;    -   (d) a polypeptide having at least 80% sequence identity to the        polypeptide of SEQ ID NO: 18;    -   (e) a polypeptide having at least 80% sequence identity to the        polypeptide of SEQ ID NO: 21;    -   (f) a polypeptide having at least 80% sequence identity to the        polypeptide of SEQ ID NO: 24;    -   (g) a polypeptide having at least 80% sequence identity to the        polypeptide of SEQ ID NO: 27;    -   (h) a polypeptide having at least 80% sequence identity to the        polypeptide of SEQ ID NO: 30;    -   (i) a polypeptide having at least 80% sequence identity to the        polypeptide of SEQ ID NO: 36;    -   (j) a polypeptide having at least 80% sequence identity to the        polypeptide of SEQ ID NO: 42;    -   (k) a polypeptide having at least 80% sequence identity to the        polypeptide of SEQ ID NO: 48;    -   (l) a polypeptide having at least 80% sequence identity to the        polypeptide of SEQ ID NO: 54;    -   (m) a polypeptide having at least 80% sequence identity to the        polypeptide of SEQ ID NO: 60;    -   (n) a polypeptide having at least 80% sequence identity to the        polypeptide of SEQ ID NO: 66;    -   (o) a polypeptide having at least 80% sequence identity to the        polypeptide of SEQ ID NO: 105;    -   (p) a polypeptide having at least 80% sequence identity to the        polypeptide of SEQ ID NO: 108;    -   (q) a polypeptide having at least 80% sequence identity to the        polypeptide of SEQ ID NO: 114;    -   (r) a polypeptide having at least 80% sequence identity to the        polypeptide of SEQ ID NO: 120;    -   (s) a polypeptide having at least 80% sequence identity to the        polypeptide of SEQ ID NO: 123;    -   (t) a polypeptide having at least 80% sequence identity to the        polypeptide of SEQ ID NO: 126;    -   (u) a polypeptide having at least 80% sequence identity to the        polypeptide of SEQ ID NO: 132;    -   (v) a polypeptide having at least 80% sequence identity to the        polypeptide of SEQ ID NO: 138;    -   (w) a polypeptide having at least 80% sequence identity to the        polypeptide of SEQ ID NO: 141;    -   (x) a polypeptide having at least 80% sequence identity to the        polypeptide of SEQ ID NO: 147;    -   (y) a polypeptide having at least 80% sequence identity to the        polypeptide of SEQ ID NO: 150;    -   (z) a polypeptide having at least 80% sequence identity to the        polypeptide of SEQ ID NO: 156;    -   (aa) a polypeptide having at least 80% sequence identity to the        polypeptide of SEQ ID NO: 159;    -   (ab) a polypeptide having at least 80% sequence identity to the        polypeptide of SEQ ID NO: 162;    -   (ac) a polypeptide having at least 80% sequence identity to the        polypeptide of SEQ ID NO: 165;    -   (ad) a polypeptide having at least 80% sequence identity to the        polypeptide of SEQ ID NO: 168;    -   (ae) a polypeptide having at least 80% sequence identity to the        polypeptide of SEQ ID NO: 171;    -   (af) a polypeptide having at least 80% sequence identity to the        polypeptide of SEQ ID NO: 174;    -   (ag) a variant of the polypeptide selected from the group        consisting of SEQ ID NO: 9, SEQ ID NO: 12, SEQ ID NO: 15, SEQ ID        NO: 18, SEQ ID NO: 21, SEQ ID NO: 24, SEQ ID NO: 27, SEQ ID NO:        30, SEQ ID NO: 36, SEQ ID NO: 42, SEQ ID NO: 48, SEQ ID NO: 54,        SEQ ID NO: 60, SEQ ID NO: 66 SEQ ID NO: 105, SEQ ID NO: 108, SEQ        ID NO: 114, SEQ ID NO: 120, SEQ ID NO: 123, SEQ ID NO: 126, SEQ        ID NO: 132, SEQ ID NO: 138, SEQ ID NO: 141, SEQ ID NO: 147, SEQ        ID NO: 150, SEQ ID NO: 156, SEQ ID NO: 159, SEQ ID NO: 162, SEQ        ID NO: 165, SEQ ID NO: 168, SEQ ID NO: 171 and SEQ ID NO: 174        wherein the variant has arabinofuranosidase activity and        comprises one or more amino acid substitutions, and/or one or        more amino acid deletions, and/or one or more amino acid        insertions or any combination thereof in 1, 2, 3, 4, 5, 6, 7, 8,        9 or 10 positions;    -   (ah) a polypeptide comprising the polypeptide of (a), (b), (c),        (d), (e), (f), (g), (h), (i), (j), (k), (l), (m), (n), (o), (p),        (q), (r), (s), (t), (u), (v), (w), (x), (y), (z), (aa), (ab),        (ac), (ad), (ae), (af) or (ag) and a N-terminal and/or        C-terminal His-tag and/or HQ-tag; and    -   (ai) a fragment of the polypeptide of (a), (b), (c), (d), (e),        (f), (g), (h), (i), (j), (k), (l), (m), (n), (o), (p), (q), (r),        (s), (t), (u), (v), (w), (x), (y), (z), (aa), (ab), (ac), (ad),        (ae), (af), (ag) or (ah) having arabinofuranosidase activity and        having at least 90% of the length of the mature polypeptide.-   4. The composition according to item 3, wherein the GH62 polypeptide    having arabinofuranosidase activity comprises or consists of amino    acids 1 to 302 of SEQ ID NO: 9, amino acids 1 to 303 of SEQ ID NO:    12, amino acids 1 to 382 of SEQ ID NO: 15, amino acids 1 to 378 of    SEQ ID NO: 18, amino acids 1 to 311 of SEQ ID NO: 21, amino acids 1    to 302 of SEQ ID NO: 24, amino acids 1 to 309 of SEQ ID NO: 27,    amino acids 1 to 438 of SEQ ID NO: 30, amino acids 1 to 446 of SEQ    ID NO: 33, amino acids 1 to 438 of SEQ ID NO: 36, amino acids 1 to    446 of SEQ ID NO: 39, amino acids 1 to 318 of SEQ ID NO: 42, amino    acids 1 to 326 of SEQ ID NO: 45, amino acids 1 to 302 of SEQ ID NO:    48, amino acids 1 to 311 of SEQ ID NO: 51, amino acids 1 to 364 of    SEQ ID NO: 54, amino acids 1 to 373 of SEQ ID NO: 57, amino acids 1    to 436 of SEQ ID NO: 60, amino acids 1 to 444 of SEQ ID NO: 63,    amino acids 1 to 302 of SEQ ID NO: 66, amino acids 1 to 311 of SEQ    ID NO: 69, amino acids 1 to 302 of SEQ ID NO: 105, amino acids 1 to    464 of SEQ ID NO: 108, amino acids 1 to 472 of SEQ ID NO: 111, amino    acids 1 to 364 of SEQ ID NO: 114, amino acids 1 to 372 of SEQ ID NO:    117, amino acids 1 to 357 of SEQ ID NO: 120, amino acids 1 to 302 of    SEQ ID NO: 123, amino acids 1 to 453 of SEQ ID NO: 126, amino acids    1 to 461 of SEQ ID NO: 129, amino acids 1 to 377 of SEQ ID NO: 132,    amino acids 1 to 385 of SEQ ID NO: 135, amino acids 1 to 309 of SEQ    ID NO: 138, amino acids 1 to 304 of SEQ ID NO: 141, amino acids 1 to    312 of SEQ ID NO: 144, amino acids 1 to 302 of SEQ ID NO: 147, amino    acids 1 to 302 of SEQ ID NO: 150, amino acids 1 to 310 of SEQ ID NO:    153, amino acids 1 to 316 of SEQ ID NO: 156, amino acids 1 to 316 of    SEQ ID NO: 159, amino acids 1 to 303 of SEQ ID NO: 162, amino acids    1 to 361 of SEQ ID NO: 165, amino acids 1 to 373 of SEQ ID NO: 168,    amino acids 1 to 302 of SEQ ID NO: 171 or amino acids 1 to 364 of    SEQ ID NO: 174.-   5. The composition of any of items 1 to 4, wherein the GH10 or GH11    polypeptide having xylanase activity is selected from the group    consisting of:    -   (a) a polypeptide having at least 80% sequence identity to the        polypeptide of SEQ ID NO: 70;    -   (b) a polypeptide having at least 80% sequence identity to the        polypeptide of SEQ ID NO: 71;    -   (c) a polypeptide having at least 80% sequence identity to the        polypeptide of SEQ ID NO: 72;    -   (d) a polypeptide having at least 80% sequence identity to the        polypeptide of SEQ ID NO: 73;    -   (e) a polypeptide having at least 80% sequence identity to the        polypeptide of SEQ ID NO: 74;    -   (f) a polypeptide having at least 80% sequence identity to the        polypeptide of SEQ ID NO: 75;    -   (g) a polypeptide having at least 80% sequence identity to the        polypeptide of SEQ ID NO: 78;    -   (h) a polypeptide having at least 80% sequence identity to the        polypeptide of SEQ ID NO: 81;    -   (i) a polypeptide having at least 80% sequence identity to the        polypeptide of SEQ ID NO: 84;    -   (j) a polypeptide having at least 80% sequence identity to the        polypeptide of SEQ ID NO: 88;    -   (k) a polypeptide having at least 80% sequence identity to the        polypeptide of SEQ ID NO: 89;    -   (l) a polypeptide having at least 80% sequence identity to the        polypeptide of SEQ ID NO: 95;    -   (m) a polypeptide having at least 80% sequence identity to the        polypeptide of SEQ ID NO: 96;    -   (n) a polypeptide having at least 80% sequence identity to the        polypeptide of SEQ ID NO: 99;    -   (o) a polypeptide having at least 80% sequence identity to the        polypeptide of SEQ ID NO: 102;    -   (p) a polypeptide having at least 80% sequence identity to the        polypeptide of SEQ ID NO: 177;    -   (q) a variant of the polypeptide selected from the group        consisting of SEQ ID NO: 70, SEQ ID NO: 71, SEQ ID NO: 72, SEQ        ID NO: 73, SEQ ID NO: 74, SEQ ID NO: 75, SEQ ID NO: 78, SEQ ID        NO: 81, SEQ ID NO: 84, SEQ ID NO: 88, SEQ ID NO: 89, SEQ ID NO:        95, SEQ ID NO: 96, SEQ ID NO: 99, SEQ ID NO: 102 and SEQ ID NO:        177 wherein the variant has xylanase activity and comprises one        or more amino acid substitutions, and/or one or more amino acid        deletions, and/or one or more amino acid insertions or any        combination thereof in 1, 2, 3, 4, 5, 6, 7, 8, 9 or 10        positions;    -   (r) a polypeptide comprising the polypeptide of (a), (b), (c),        (d), (e), (f), (g), (h), (i), (j), (k), (l), (m), (n), (o), (p)        or (q) and a N-terminal and/or C-terminal His-tag and/or HQ-tag;        and    -   (s) a fragment of the polypeptide of (a), (b), (c), (d), (e),        (f), (g), (h), (i), (j), (k), (l), (m), (n), (o), (p), (q)        or (r) having xylanase activity and having at least 90% of the        length of the mature polypeptide.-   6. The composition according to item 5, wherein the GH10 or GH11    polypeptide comprises or consists of amino acids 1 to 384 of SEQ ID    NO: 70, amino acids 1 to 288 of SEQ ID NO: 71, amino acids 1 to 308    of SEQ ID NO: 72, amino acids 1 to 195 of SEQ ID NO: 73, amino acids    1 to 203 of SEQ ID NO: 74, amino acids 1 to 182 of SEQ ID NO: 75,    amino acids 1 to 183 of SEQ ID NO: 78, amino acids 1 to 181 of SEQ    ID NO: 81, amino acids 1 to 299 of SEQ ID NO: 84, amino acids 1 to    307 of SEQ ID NO: 87, amino acids 1 to 188 of SEQ ID NO: 88, amino    acids 1 to 189 of SEQ ID NO: 89, amino acids 1 to 328 of SEQ ID NO:    95, amino acids 1 to 208 of SEQ ID NO:96, amino acids 1 to 203 of    SEQ ID NO:99, amino acids 1 to 337 of SEQ ID NO:102 or amino acids 1    to 323 of SEQ ID NO: 177.-   7. The composition of any of items 1 to 6, wherein the GH10 or GH11    polypeptide and the GH62 polypeptide together solubilise at least    0.4% xylose from DFDSM and the GH10 or GH11 polypeptide and the GH62    polypeptide together solubilise at least 2.5 times more xylose from    DFDSM than the GH10 or GH11 polypeptide can when the GH62    polypeptide is not present.-   8. The composition of any of items 1 to 6, wherein the GH10 or GH11    polypeptide and the GH62 polypeptide together solubilise at least    0.4% xylose from DFDSM and the GH10 or GH11 polypeptide and the GH62    polypeptide together solubilise at least 3 times more xylose from    DFDSM than the GH10 or GH11 polypeptide can when the GH62    polypeptide is not present.-   9. The composition of any of items 1 to 6, wherein the GH10 or GH11    polypeptide and the GH62 polypeptide together solubilise at least    0.4% xylose from DFDSM and the GH10 or GH11 polypeptide and the GH62    polypeptide together solubilise at least 3.5 times more xylose from    DFDSM than the GH10 or GH11 polypeptide can when the GH62    polypeptide is not present.-   10. The composition of any of items 1 to 6, wherein the GH10 or GH11    polypeptide and the GH62 polypeptide together solubilise at least    0.4% xylose from DFDSM and the GH10 or GH11 polypeptide and the GH62    polypeptide together solubilise at least 4 times more xylose from    DFDSM than the GH10 or GH11 polypeptide can when the GH62    polypeptide is not present.-   11. The composition of any of items 1 to 6, wherein the GH10 or GH11    polypeptide and the GH62 polypeptide together solubilise at least    0.6% xylose from DFDSM and the GH10 or GH11 polypeptide and the GH62    polypeptide together solubilise at least 2 times more xylose from    DFDSM than the GH10 or GH11 polypeptide can when the GH62    polypeptide is not present.-   12. The composition of any of items 1 to 6, wherein the GH10 or GH11    polypeptide and the GH62 polypeptide together solubilise at least    0.6% xylose from DFDSM and the GH10 or GH11 polypeptide and the GH62    polypeptide together solubilise at least 2.5 times more xylose from    DFDSM than the GH10 or GH11 polypeptide can when the GH62    polypeptide is not present.-   13. The composition of any of items 1 to 6, wherein the GH10 or GH11    polypeptide and the GH62 polypeptide together solubilise at least    0.6% xylose from DFDSM and the GH10 or GH11 polypeptide and the GH62    polypeptide together solubilise at least 3 times more xylose from    DFDSM than the GH10 or GH11 polypeptide can when the GH62    polypeptide is not present.-   14. The composition of any of items 1 to 6, wherein the GH10 or GH11    polypeptide and the GH62 polypeptide together solubilise at least    0.6% xylose from DFDSM and the GH10 or GH11 polypeptide and the GH62    polypeptide together solubilise at least 3.5 times more xylose from    DFDSM than the GH10 or GH11 polypeptide can when the GH62    polypeptide is not present.-   15. The composition of any of items 1 to 6, wherein the GH10 or GH11    polypeptide and the GH62 polypeptide together solubilise at least    0.8% xylose from DFDSM and the GH10 or GH11 polypeptide and the GH62    polypeptide together solubilise at least 2 times more xylose from    DFDSM than the GH10 or GH11 polypeptide can when the GH62    polypeptide is not present.-   16. The composition of any of items 1 to 6, wherein the GH10 or GH11    polypeptide and the GH62 polypeptide together solubilise at least    0.8% xylose from DFDSM and the GH10 or GH11 polypeptide and the GH62    polypeptide together solubilise at least 2.5 times more xylose from    DFDSM than the GH10 or GH11 polypeptide can when the GH62    polypeptide is not present.-   17. The composition of any of items 1 to 6, wherein the GH10 or GH11    polypeptide and the GH62 polypeptide together solubilise at least    0.8% xylose from DFDSM and the GH10 or GH11 polypeptide and the GH62    polypeptide together solubilise at least 3 times more xylose from    DFDSM than the GH10 or GH11 polypeptide can when the GH62    polypeptide is not present.-   18. The composition of any of items 1 to 6, wherein the GH10 or GH11    polypeptide and the GH62 polypeptide together solubilise at least    0.8% xylose from DFDSM and the GH10 or GH11 polypeptide and the GH62    polypeptide together solubilise at least 3.5 times more xylose from    DFDSM than the GH10 or GH11 polypeptide can when the GH62    polypeptide is not present.-   19. The composition of any of items 1 to 6, wherein the GH10 or GH11    polypeptide and the GH62 polypeptide together solubilise at least    1.0% xylose from DFDSM and the GH10 or GH11 polypeptide and the GH62    polypeptide together solubilise at least 2 times more xylose from    DFDSM than the GH10 or GH11 polypeptide can when the GH62    polypeptide is not present.-   20. The composition of any of items 1 to 6, wherein the GH10 or GH11    polypeptide and the GH62 polypeptide together solubilise at least    1.0% xylose from DFDSM and the GH10 or GH11 polypeptide and the GH62    polypeptide together solubilise at least 2.5 times more xylose from    DFDSM than the GH10 or GH11 polypeptide can when the GH62    polypeptide is not present.-   21. The composition of any of items 1 to 6, wherein the GH10 or GH11    polypeptide and the GH62 polypeptide together solubilise at least    1.0% xylose from DFDSM and the GH10 or GH11 polypeptide and the GH62    polypeptide together solubilise at least 3 times more xylose from    DFDSM than the GH10 or GH11 polypeptide can when the GH62    polypeptide is not present.-   22. The composition of any of items 1 to 6, wherein the GH10 or GH11    polypeptide and the GH62 polypeptide together solubilise at least    1.0% xylose from DFDSM and the GH10 or GH11 polypeptide and the GH62    polypeptide together solubilise at least 3.5 times more xylose from    DFDSM than the GH10 or GH11 polypeptide can when the GH62    polypeptide is not present.-   23. An isolated polypeptide having arabinofuranosidase activity,    selected from the group consisting of:    -   (a) a polypeptide having at least 85% sequence identity to the        polypeptide of SEQ ID NO: 12;    -   (b) a polypeptide having at least 97.6% sequence identity to the        polypeptide of SEQ ID NO: 24;    -   (c) a polypeptide having at least 80% sequence identity to the        polypeptide of SEQ ID NO: 27;    -   (d) a polypeptide having at least 90% sequence identity to the        polypeptide of SEQ ID NO: 30;    -   (e) a polypeptide having at least 92% sequence identity to the        polypeptide of SEQ ID NO: 36;    -   (f) a polypeptide having at least 86% sequence identity to the        polypeptide of SEQ ID NO:48;    -   (g) a polypeptide having at least 80% sequence identity to the        polypeptide of SEQ ID NO:54;    -   (h) a polypeptide having at least 81% sequence identity to the        polypeptide of SEQ ID NO:60;    -   (i) a polypeptide having at least 84% sequence identity to the        polypeptide of SEQ ID NO:66;    -   (j) a polypeptide having at least 87% sequence identity to the        polypeptide of SEQ ID NO:105;    -   (k) a polypeptide having at least 85% sequence identity to the        polypeptide of SEQ ID NO:108;    -   (l) a polypeptide having at least 80% sequence identity to the        polypeptide of SEQ ID NO:114;    -   (m) a polypeptide having at least 80% sequence identity to the        polypeptide of SEQ ID NO:120;    -   (n) a polypeptide having at least 89% sequence identity to the        polypeptide of SEQ ID NO:123;    -   (o) a polypeptide having at least 80% sequence identity to the        polypeptide of SEQ ID NO:126;    -   (p) a polypeptide having at least 85% sequence identity to the        polypeptide of SEQ ID NO:138;    -   (q) a polypeptide having at least 89% sequence identity to the        polypeptide of SEQ ID NO:141;    -   (r) a polypeptide having at least 86% sequence identity to the        polypeptide of SEQ ID NO:147;    -   (s) a polypeptide having at least 96.4% sequence identity to the        polypeptide of SEQ ID NO:156;    -   (t) a polypeptide having at least 80% sequence identity to the        polypeptide of SEQ ID NO:162;    -   (u) a polypeptide having at least 80% sequence identity to the        polypeptide of SEQ ID NO:165;    -   (v) a polypeptide having at least 80% sequence identity to the        polypeptide of SEQ ID NO:168;    -   (w) a polypeptide having at least 80% sequence identity to the        polypeptide of SEQ ID NO:171;    -   (x) a polypeptide having at least 82% sequence identity to the        polypeptide of SEQ ID NO: 174;    -   (y) a polypeptide encoded by a polynucleotide that hybridizes        under high stringency conditions, or very high stringency        conditions with        -   (i) the mature polypeptide coding sequence of SEQ ID NO: 10,        -   (ii) the mature polypeptide coding sequence of SEQ ID NO:            22,        -   (iii) the mature polypeptide coding sequence of SEQ ID NO:            25,        -   (iv) the mature polypeptide coding sequence of SEQ ID NO:            28,        -   (v) the mature polypeptide coding sequence of SEQ ID NO: 34,        -   (vi) the mature polypeptide coding sequence of SEQ ID NO:            46,        -   (vii) the mature polypeptide coding sequence of SEQ ID NO:            52,        -   (viii) the mature polypeptide coding sequence of SEQ ID NO:            58,        -   (ix) the mature polypeptide coding sequence of SEQ ID NO:            64,        -   (x) the mature polypeptide coding sequence of SEQ ID NO:            103,        -   (xi) the mature polypeptide coding sequence of SEQ ID NO:            106,        -   (xii) the mature polypeptide coding sequence of SEQ ID NO:            112,        -   (xiii) the mature polypeptide coding sequence of SEQ ID NO:            118,        -   (xiv) the mature polypeptide coding sequence of SEQ ID NO:            121,        -   (xv) the mature polypeptide coding sequence of SEQ ID NO:            124,        -   (xvi) the mature polypeptide coding sequence of SEQ ID NO:            136,        -   (xvii) the mature polypeptide coding sequence of SEQ ID NO:            139,        -   (xviii) the mature polypeptide coding sequence of SEQ ID NO:            145,        -   (xix) the mature polypeptide coding sequence of SEQ ID NO:            154,        -   (xx) the mature polypeptide coding sequence of SEQ ID NO:            160,        -   (xxi) the mature polypeptide coding sequence of SEQ ID NO:            163,        -   (xxii) the mature polypeptide coding sequence of SEQ ID NO:            166,        -   (xxiii) the mature polypeptide coding sequence of SEQ ID NO:            169,        -   (xxiv) the mature polypeptide coding sequence of SEQ ID NO:            172,        -   (xxv) the full-length complementary strand of (i), (ii),            (iii), (iv), (v), (vi), (vii), (viii), (ix), (x), (xi),            (xii), (xiii), (xiv), (xv), (xvi), (xvii), (xviii), (xix),            (xx), (xxi), (xxii), (xxiii) or (xxiv);    -   (z) a polypeptide encoded by a polynucleotide having at least        85% sequence identity to the mature polypeptide coding sequence        of SEQ ID NO: 10;    -   (aa) a polypeptide encoded by a polynucleotide having at least        97.6% sequence identity to the mature polypeptide coding        sequence of SEQ ID NO: 22;    -   (ab) a polypeptide encoded by a polynucleotide having at least        80% sequence identity to the mature polypeptide coding sequence        of SEQ ID NO: 25;    -   (ac) a polypeptide encoded by a polynucleotide having at least        90% sequence identity to the mature polypeptide coding sequence        of SEQ ID NO: 28;    -   (ad) a polypeptide encoded by a polynucleotide having at least        92% sequence identity to the mature polypeptide coding sequence        of SEQ ID NO: 34;    -   (ae) a polypeptide encoded by a polynucleotide having at least        86% sequence identity to the mature polypeptide coding sequence        of SEQ ID NO: 46;    -   (af) a polypeptide encoded by a polynucleotide having at least        80% sequence identity to the mature polypeptide coding sequence        of SEQ ID NO: 52;    -   (ag) a polypeptide encoded by a polynucleotide having at least        81% sequence identity to the mature polypeptide coding sequence        of SEQ ID NO: 58;    -   (ah) a polypeptide encoded by a polynucleotide having at least        84% sequence identity to the mature polypeptide coding sequence        of SEQ ID NO: 64;    -   (ai) a polypeptide encoded by a polynucleotide having at least        87% sequence identity to the mature polypeptide coding sequence        of SEQ ID NO: 103;    -   (aj) a polypeptide encoded by a polynucleotide having at least        85% sequence identity to the mature polypeptide coding sequence        of SEQ ID NO: 106;    -   (ak) a polypeptide encoded by a polynucleotide having at least        80% sequence identity to the mature polypeptide coding sequence        of SEQ ID NO: 111;    -   (al) a polypeptide encoded by a polynucleotide having at least        80% sequence identity to the mature polypeptide coding sequence        of SEQ ID NO: 118;    -   (am) a polypeptide encoded by a polynucleotide having at least        89% sequence identity to the mature polypeptide coding sequence        of SEQ ID NO: 121;    -   (an) a polypeptide encoded by a polynucleotide having at least        80% sequence identity to the mature polypeptide coding sequence        of SEQ ID NO: 124;    -   (ao) a polypeptide encoded by a polynucleotide having at least        85% sequence identity to the mature polypeptide coding sequence        of SEQ ID NO: 136;    -   (ap) a polypeptide encoded by a polynucleotide having at least        89% sequence identity to the mature polypeptide coding sequence        of SEQ ID NO: 139;    -   (aq) a polypeptide encoded by a polynucleotide having at least        86% sequence identity to the mature polypeptide coding sequence        of SEQ ID NO: 145;    -   (ar) a polypeptide encoded by a polynucleotide having at least        96.4% sequence identity to the mature polypeptide coding        sequence of SEQ ID NO: 154;    -   (as) a polypeptide encoded by a polynucleotide having at least        80% sequence identity to the mature polypeptide coding sequence        of SEQ ID NO: 160;    -   (at) a polypeptide encoded by a polynucleotide having at least        80% sequence identity to the mature polypeptide coding sequence        of SEQ ID NO: 163;    -   (au) a polypeptide encoded by a polynucleotide having at least        80% sequence identity to the mature polypeptide coding sequence        of SEQ ID NO: 166;    -   (av) a polypeptide encoded by a polynucleotide having at least        80% sequence identity to the mature polypeptide coding sequence        of SEQ ID NO: 169;    -   (aw) a polypeptide encoded by a polynucleotide having at least        82% sequence identity to the mature polypeptide coding sequence        of SEQ ID NO: 172;    -   (ax) a variant of SEQ ID NO: 12, wherein the variant has        arabinofuranosidase activity and comprises one or more amino        acid substitutions, and/or one or more amino acid deletions,        and/or one or more amino acid insertions or any combination        thereof in 1, 2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, 15,        16, 17, 18, 19, 20, 21, 22, 23, 24, 25, 26, 27, 28, 29, 30, 31,        32, 33, 34, 35, 36, 37, 38, 39, 40, 41, 42, 43, 44 or 45        positions;    -   (ay) a variant of SEQ ID NO: 24, wherein the variant has        arabinofuranosidase activity and comprises one or more amino        acid substitutions, and/or one or more amino acid deletions,        and/or one or more amino acid insertions or any combination        thereof in 1, 2, 3, 4, 5, 6 or 7 positions;    -   (az) a variant of the polypeptide selected from the group        consisting of SEQ ID NO: 27, SEQ ID NO: 54, SEQ ID NO: 60, SEQ        ID NO: 108, SEQ ID NO: 114, SEQ ID NO: 120, SEQ ID NO: 126, SEQ        ID NO: 162, SEQ ID NO: 165, SEQ ID NO: 168, SEQ ID NO: 171 or        SEQ ID NO: 174 wherein the variant has arabinofuranosidase        activity and comprises one or more amino acid substitutions,        and/or one or more amino acid deletions, and/or one or more        amino acid insertions or any combination thereof in 1, 2, 3, 4,        5, 6, 7, 8, 9, 10, 11, 12, 13, 14, 15, 16, 17, 18, 19, 20, 21,        22, 23, 24, 25, 26, 27, 28, 29, 30, 31, 32, 33, 34, 35, 36, 37,        38, 39, 40, 41, 42, 43, 44, 45, 46, 47, 48, 49 or 50 positions;    -   (ba) a variant of SEQ ID NO: 30, wherein the variant has        arabinofuranosidase activity and comprises one or more amino        acid substitutions, and/or one or more amino acid deletions,        and/or one or more amino acid insertions or any combination        thereof in 1, 2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, 15,        16, 17, 18, 19, 20, 21, 22, 23, 24, 25, 26, 27, 28, 29, 30, 31,        32, 33, 34, 35, 36, 37, 38, 39, 40, 41, 42 or 43 positions;    -   (bb) a variant of SEQ ID NO: 36, wherein the variant has        arabinofuranosidase activity and comprises one or more amino        acid substitutions, and/or one or more amino acid deletions,        and/or one or more amino acid insertions or any combination        thereof in 1, 2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, 15,        16, 17, 18, 19, 20, 21, 22, 23, 24, 25, 26, 27, 28, 29, 30, 31,        32, 33 or 34 positions;    -   (bc) a variant of the polypeptide selected from the group        consisting of SEQ ID NO: 48 or SEQ ID NO: 147 wherein the        variant has arabinofuranosidase activity and comprises one or        more amino acid substitutions, and/or one or more amino acid        deletions, and/or one or more amino acid insertions or any        combination thereof in 1, 2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12,        13, 14, 15, 16, 17, 18, 19, 20, 21, 22, 23, 24, 25, 26, 27, 28,        29, 30, 31, 32, 33, 34, 35, 36, 37, 38, 39, 40, 41 or 42        positions;    -   (bd) a variant of SEQ ID NO: 66, wherein the variant has        arabinofuranosidase activity and comprises one or more amino        acid substitutions, and/or one or more amino acid deletions,        and/or one or more amino acid insertions or any combination        thereof in 1, 2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, 15,        16, 17, 18, 19, 20, 21, 22, 23, 24, 25, 26, 27, 28, 29, 30, 31,        32, 33, 34, 35, 36, 37, 38, 39, 40, 41, 42, 43, 44, 45, 46, 47        or 48 positions;    -   (be) a variant of SEQ ID NO: 105, wherein the variant has        arabinofuranosidase activity and comprises one or more amino        acid substitutions, and/or one or more amino acid deletions,        and/or one or more amino acid insertions or any combination        thereof in 1, 2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, 15,        16, 17, 18, 19, 20, 21, 22, 23, 24, 25, 26, 27, 28, 29, 30, 31,        32, 33, 34, 35, 36, 37, 38 or 39 positions;    -   (bf) a variant of the polypeptide selected from the group        consisting of SEQ ID NO: 123 or SEQ ID NO: 141 wherein the        variant has arabinofuranosidase activity and comprises one or        more amino acid substitutions, and/or one or more amino acid        deletions, and/or one or more amino acid insertions or any        combination thereof in 1, 2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12,        13, 14, 15, 16, 17, 18, 19, 20, 21, 22, 23, 24, 25, 26, 27, 28,        29, 30, 31, 32 or 33 positions;    -   (bg) a variant of SEQ ID NO: 138, wherein the variant has        arabinofuranosidase activity and comprises one or more amino        acid substitutions, and/or one or more amino acid deletions,        and/or one or more amino acid insertions or any combination        thereof in 1, 2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, 15,        16, 17, 18, 19, 20, 21, 22, 23, 24, 25, 26, 27, 28, 29, 30, 31,        32, 33, 34, 35, 36, 37, 38, 39, 40, 41, 42, 43, 44, 45 or 46        positions;    -   (bh) a variant of SEQ ID NO: 156, wherein the variant has        arabinofuranosidase activity and comprises one or more amino        acid substitutions, and/or one or more amino acid deletions,        and/or one or more amino acid insertions or any combination        thereof in 1, 2, 3, 4, 5, 6, 7, 8, 9, 10 or 11 positions;    -   (bi) a polypeptide comprising the polypeptide of (a), (b), (c),        (d), (e), (f), (g), (h), (i), (j), (k), (l), (m), (n), (o), (p),        (q), (r), (s), (t), (u), (v), (w), (x), (y), (z), (aa), (ab),        (ac), (ad), (ae), (af), (ag), (ah), (ai), (aj), (ak), (al),        (am), (an), (ao), (ap), (aq), (ar), (as), (at), (au), (av),        (aw), (ax), (ay), (az), (ba), (bb), (bc), (bd), (be), (bf), (bg)        or (bh) and a N-terminal and/or C-terminal His-tag and/or        HQ-tag; and    -   (bj) a fragment of the polypeptide of (a), (b), (c), (d), (e),        (f), (g), (h), (i), (j), (k), (l), (m), (n), (o), (p), (q), (r),        (s), (t), (u), (v), (w), (x), (y), (z), (aa), (ab), (ac), (ad),        (ae), (af), (ag), (ah), (ai), (aj), (ak), (al), (am), (an),        (ao), (ap), (aq), (ar), (as), (at), (au), (av), (aw), (ax),        (ay), (az), (ba), (bb), (bc), (bd), (be), (bf), (bg), (bh) or        (bi) having arabinofuranosidase activity and having at least 90%        of the length of the mature polypeptide.-   24. The polypeptide according to item 23, wherein the polypeptide    comprises or consists of amino acids 1 to 303 of SEQ ID NO: 12,    amino acids 1 to 302 of SEQ ID NO: 24, amino acids 1 to 309 of SEQ    ID NO: 27, amino acids 1 to 438 of SEQ ID NO: 30, amino acids 1 to    446 of SEQ ID NO: 33, amino acids 1 to 438 of SEQ ID NO: 36, amino    acids 1 to 446 of SEQ ID NO: 39, amino acids 1 to 302 of SEQ ID NO:    48, amino acids 1 to 311 of SEQ ID NO: 51, amino acids 1 to 364 of    SEQ ID NO: 54, amino acids 1 to 373 of SEQ ID NO: 57, amino acids 1    to 436 of SEQ ID NO: 60, amino acids 1 to 444 of SEQ ID NO: 63,    amino acids 1 to 302 of SEQ ID NO: 66, amino acids 1 to 311 of SEQ    ID NO: 69, amino acids 1 to 302 of SEQ ID NO: 105, amino acids 1 to    464 of SEQ ID NO: 108, amino acids 1 to 472 of SEQ ID NO: 111, amino    acids 1 to 364 of SEQ ID NO: 114, amino acids 1 to 372 of SEQ ID NO:    117, amino acids 1 to 357 of SEQ ID NO: 120, amino acids 1 to 302 of    SEQ ID NO: 123, amino acids 1 to 453 of SEQ ID NO: 126, amino acids    1 to 461 of SEQ ID NO: 129, amino acids 1 to 309 of SEQ ID NO: 138,    amino acids 1 to 304 of SEQ ID NO: 141, amino acids 1 to 312 of SEQ    ID NO: 144, amino acids 1 to 302 of SEQ ID NO: 147, amino acids 1 to    316 of SEQ ID NO: 156, amino acids 1 to 303 of SEQ ID NO: 162, amino    acids 1 to 361 of SEQ ID NO: 165, amino acids 1 to 373 of SEQ ID NO:    168, amino acids 1 to 302 of SEQ ID NO: 171 or amino acids 1 to 364    of SEQ ID NO: 174.-   25. A composition comprising one or more polypeptides of any of    items 23 to 24.-   26. The composition of item 25 further comprising one or more GH10    or GH11 polypeptides having xylanase activity.-   27. The composition of item 26, wherein the GH10 or GH11 polypeptide    having xylanase activity is selected from the group consisting of:    -   (a) a polypeptide having at least 80% sequence identity to the        polypeptide of SEQ ID NO: 70;    -   (b) a polypeptide having at least 80% sequence identity to the        polypeptide of SEQ ID NO: 71;    -   (c) a polypeptide having at least 80% sequence identity to the        polypeptide of SEQ ID NO: 72;    -   (d) a polypeptide having at least 80% sequence identity to the        polypeptide of SEQ ID NO: 73;    -   (e) a polypeptide having at least 80% sequence identity to the        polypeptide of SEQ ID NO: 74;    -   (f) a polypeptide having at least 80% sequence identity to the        polypeptide of SEQ ID NO: 75;    -   (g) a polypeptide having at least 80% sequence identity to the        polypeptide of SEQ ID NO: 78;    -   (h) a polypeptide having at least 80% sequence identity to the        polypeptide of SEQ ID NO: 81;    -   (i) a polypeptide having at least 80% sequence identity to the        polypeptide of SEQ ID NO: 84;    -   (j) a polypeptide having at least 80% sequence identity to the        polypeptide of SEQ ID NO: 88;    -   (k) a polypeptide having at least 80% sequence identity to the        polypeptide of SEQ ID NO: 89;    -   (l) a polypeptide having at least 80% sequence identity to the        polypeptide of SEQ ID NO: 95;    -   (m) a polypeptide having at least 80% sequence identity to the        polypeptide of SEQ ID NO: 96;    -   (n) a polypeptide having at least 80% sequence identity to the        polypeptide of SEQ ID NO: 99;    -   (o) a polypeptide having at least 80% sequence identity to the        polypeptide of SEQ ID NO: 102;    -   (p) a polypeptide having at least 80% sequence identity to the        polypeptide of SEQ ID NO: 177;    -   (q) a variant of the polypeptide selected from the group        consisting of SEQ ID NO: 70, SEQ ID NO: 71, SEQ ID NO: 72, SEQ        ID NO: 73, SEQ ID NO: 74, SEQ ID NO: 75, SEQ ID NO: 78, SEQ ID        NO: 81, SEQ ID NO: 84, SEQ ID NO: 88, SEQ ID NO: 89, SEQ ID NO:        95, SEQ ID NO: 96, SEQ ID NO: 99, SEQ ID NO: 102 and SEQ ID NO:        177 wherein the variant has xylanase activity and comprises one        or more amino acid substitutions, and/or one or more amino acid        deletions, and/or one or more amino acid insertions or any        combination thereof in 1, 2, 3, 4, 5, 6, 7, 8, 9 or 10        positions;    -   (r) a polypeptide comprising the polypeptide of (a), (b), (c),        (d), (e), (f), (g), (h), (i), (j), (k), (l), (m), (n), (o), (p)        or (q) and a N-terminal and/or C-terminal His-tag and/or HQ-tag;        and    -   (s) a fragment of the polypeptide of (a), (b), (c), (d), (e),        (f), (g), (h), (i), (j), (k), (l), (m), (n), (o), (p), (q)        or (r) having xylanase activity and having at least 90% of the        length of the mature polypeptide.-   28. The composition according to item 27, wherein the GH10 or GH11    polypeptide having xylanase activity is selected from the group    consisting of amino acids 1 to 384 of SEQ ID NO: 70, amino acids 1    to 288 of SEQ ID NO: 71, amino acids 1 to 308 of SEQ ID NO: 72,    amino acids 1 to 195 of SEQ ID NO: 73, amino acids 1 to 203 of SEQ    ID NO: 74, amino acids 1 to 182 of SEQ ID NO: 75, amino acids 1 to    183 of SEQ ID NO: 78, amino acids 1 to 181 of SEQ ID NO: 81, amino    acids 1 to 299 of SEQ ID NO: 84, amino acids 1 to 307 of SEQ ID NO:    87, amino acids 1 to 188 of SEQ ID NO: 88, amino acids 1 to 189 of    SEQ ID NO: 89, amino acids 1 to 328 of SEQ ID NO: 95, amino acids 1    to 208 of SEQ ID NO:96, amino acids 1 to 203 of SEQ ID NO:99, amino    acids 1 to 337 of SEQ ID NO:102 or amino acids 1 to 323 of SEQ ID    NO: 177.-   29. The composition of any of items 1 to 22 or 25 to 28 further    comprising one or more formulating agents.-   30. The composition of item 29, wherein the one or more formulating    agent is selected from the group consisting of glycerol, ethylene    glycol, 1,2-propylene glycol or 1,3-propylene glycol, sodium    chloride, sodium benzoate, potassium sorbate, sodium sulfate,    potassium sulfate, magnesium sulfate, sodium thiosulfate, calcium    carbonate, sodium citrate, dextrin, glucose, sucrose, sorbitol,    lactose, starch and cellulose or any combination thereof.-   31. The composition of any of items 1 to 22 or 25 to 30 further    comprising one or more additional enzymes.-   32. The composition of item 31, wherein the one or more additional    enzymes is selected from the group consisting of phytase, xylanase,    galactanase, alpha-galactosidase, protease, phospholipase A1,    phospholipase A2, lysophospholipase, phospholipase C, phospholipase    D, amylase, lysozyme, arabinofuranosidase, beta-xylosidase, acetyl    xylan esterase, feruloyl esterase, cellulase, cellobiohydrolases,    beta-glucosidase, pullulanase, and beta-glucanase or any combination    thereof.-   33. The composition of any of items 1 to 22 or 25 to 32 further    comprising one or more microbes.

34. The composition of item 33, wherein the one or more microbes isselected from the group consisting of Bacillus subtilis, Bacilluslicheniformis, Bacillus amyloliquefaciens, Bacillus cereus, Bacilluspumilus, Bacillus polymyxa, Bacillus megaterium, Bacillus coagulans,Bacillus circulans, Bifidobacterium bifidum, Bifidobacterium animalis,Bifidobacterium sp., Carnobacterium sp., Clostridium butyricum,Clostridium sp., Enterococcus faecium, Enterococcus sp., Lactobacillussp., Lactobacillus acidophilus, Lactobacillus farciminus, Lactobacillusrhamnosus, Lactobacillus reuteri, Lactobacillus salivarius, Lactococcuslactis, Lactococcus sp., Leuconostoc sp., Megasphaera elsdenii,Megasphaera sp., Pediococsus acidilactici, Pediococcus sp.,Propionibacterium thoenii, Propionibacterium sp. and Streptococcus sp.or any combination thereof.

-   35. The composition of any of items 1 to 22 or 25 to 34 further    comprising plant based material from the sub-family Panicoideae.-   36. The composition of item 35, wherein the plant based material    from the sub-family Panicoideae is maize, corn, sorghum,    switchgrass, millet, pearl millet, foxtail millet or in a processed    form such as milled corn, milled maize, defatted maize, defatted    destarched maize, milled sorghum, milled switchgrass, milled millet,    milled foxtail millet, milled pearl millet, or any combination    thereof.-   37. The composition of any of items 35 to 36, wherein the plant    based material from the sub-family Panicoideae is from the seed    fraction (such as endosperm and/or husk) of the plant.-   38. An animal feed additive comprising the composition of any of    items 1 to 22 or 25 to 34 and one or more components selected from    the list consisting of:    -   one or more vitamins;    -   one or more minerals;    -   one or more amino acids; and    -   one or more other feed ingredients.-   39. An animal feed comprising the composition of any of items 1 to    22 or 25 to 34 or the animal feed additive of item 38 and plant    based material from the sub-family Panicoideae.-   40. The animal feed of item 39, wherein the plant based material    from the sub-family Panicoideae is maize, corn, sorghum,    switchgrass, millet, pearl millet, foxtail millet or in a processed    form such as milled corn, milled maize, defatted maize, defatted    destarched maize, milled sorghum, milled switchgrass, milled millet,    milled foxtail millet, milled pearl millet, or any combination    thereof.-   41. The animal feed of any of items 39 to 40, wherein the plant    based material from the sub-family Panicoideae is from the seed    fraction (such as endosperm and/or husk) of the plant.-   42. A method of improving one or more performance parameters of an    animal comprising administering to one or more animals the    composition of any of items 1 to 22 or 25 to 37, the animal feed    additive of item 38 or an animal feed of any of items 39 to 41.-   43. The method of item 42, wherein the performance parameter is    selected from the list consisting of body weight gain, European    Production Efficiency Factor (EPEF), European Production Efficacy    Factor (EFF) and FCR.-   44. A method of solubilising xylose from plant based material,    comprising treating plant based material from the sub-family    Panicoideae with the composition of any of items 1 to 22 or 25 to 37    or the animal feed additive of item 38.-   45. A method of releasing starch from plant based material,    comprising treating plant based material from the sub-family    Panicoideae with the composition of any of items 1 to 22 or 25 to 37    or the animal feed additive of item 38.-   46. A method for improving the nutritional value of an animal feed,    comprising adding to the feed the composition of any of items 1 to    22 or 25 to 37 or the animal feed additive of item 38.-   47. A method of preparing an animal feed, comprising mixing the    composition of any of items 1 to 22 or 25 to 37 or the animal feed    additive of item 38 with plant based material from the sub-family    Panicoideae.-   48. Use of the composition of any of items 1 to 22 or 25 to 37, the    animal feed additive of item 38 or an animal feed of any of items 39    to 41:    -   in animal feed;    -   in animal feed additives;    -   in the preparation of a composition for use in animal feed;    -   for improving the nutritional value of an animal feed;    -   for increasing digestibility of the animal feed;    -   for improving one or more performance parameters in an animal;    -   for releasing xylose from plant based material of the sub-family        Panicoideae; and/or    -   for releasing starch from plant based material of the sub-family        Panicoideae.-   49. An isolated polypeptide having xylanase activity, selected from    the group consisting of:    -   (a) a polypeptide having at least 84% sequence identity to the        polypeptide of SEQ ID NO: 84;    -   (b) a polypeptide having at least 80% sequence identity to the        polypeptide of SEQ ID NO: 99;    -   (c) a polypeptide having at least 80% sequence identity to the        polypeptide of SEQ ID NO: 102;    -   (d) a polypeptide encoded by a polynucleotide that hybridizes        under high stringency conditions, or very high stringency        conditions with        -   (i) the mature polypeptide coding sequence of SEQ ID NO: 82,        -   (ii) the mature polypeptide coding sequence of SEQ ID NO:            97,        -   (iii) the mature polypeptide coding sequence of SEQ ID NO:            100,        -   (iv) the full-length complementary strand of (i), (ii) or            (iii);    -   (e) a polypeptide encoded by a polynucleotide having at least        84% sequence identity to the mature polypeptide coding sequence        of SEQ ID NO: 82;    -   (f) a polypeptide encoded by a polynucleotide having at least        80% sequence identity to the mature polypeptide coding sequence        of SEQ ID NO: 97;    -   (g) a polypeptide encoded by a polynucleotide having at least        80% sequence identity to the mature polypeptide coding sequence        of SEQ ID NO: 100;    -   (h) a variant of the polypeptide selected from the group        consisting of SEQ ID NO: 84, SEQ ID NO: 99 or SEQ ID NO: 102        wherein the variant has xylanase activity and comprises one or        more amino acid substitutions, and/or one or more amino acid        deletions, and/or one or more amino acid insertions or any        combination thereof in 1, 2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12,        13, 14, 15, 16, 17, 18, 19, 20, 21, 22, 23, 24, 25, 26, 27, 28,        29, 30, 31, 32, 33, 34, 35, 36, 37, 38, 39, 40, 41, 42, 43, 44,        45, 46, 47, 48, 49 or 50 positions;    -   (i) a polypeptide comprising the polypeptide of (a), (b), (c),        (d), (e), (f), (g), (h) or (i) and a N-terminal and/or        C-terminal His-tag and/or HQ-tag; and    -   (j) a fragment of the polypeptide of (a), (b), (c), (d), (e),        (f), (g), (h), (i) or (j) having xylanase activity and having at        least 90% of the length of the mature polypeptide.-   50. The polypeptide according to item 49, wherein the polypeptide    comprises or consists of amino acids 1 to 299 of SEQ ID NO: 84,    amino acids 1 to 307 of SEQ ID NO: 87, amino acids 1 to 203 of SEQ    ID NO:99 or amino acids 1 to 337 of SEQ ID NO:102.-   51. A composition comprising one or more polypeptides of any of    items 49 to 50.-   52. The composition of item 51 further comprising one or more    formulating agents.-   53. The composition of item 52, wherein the one or more formulating    agent is selected from the group consisting of glycerol, ethylene    glycol, 1,2-propylene glycol or 1,3-propylene glycol, sodium    chloride, sodium benzoate, potassium sorbate, sodium sulfate,    potassium sulfate, magnesium sulfate, sodium thiosulfate, calcium    carbonate, sodium citrate, dextrin, glucose, sucrose, sorbitol,    lactose, starch and cellulose or any combination thereof.-   54. The composition of any of items 51 to 53 further comprising one    or more additional enzymes.-   55. The composition of item 54, wherein the one or more additional    enzymes is selected from the group consisting of phytase, xylanase,    galactanase, alpha-galactosidase, protease, phospholipase A1,    phospholipase A2, lysophospholipase, phospholipase C, phospholipase    D, amylase, lysozyme, arabinofuranosidase, beta-xylosidase, acetyl    xylan esterase, feruloyl esterase, cellulase, cellobiohydrolases,    beta-glucosidase, pullulanase, and beta-glucanase or any combination    thereof.-   56. The composition of any of items 51 to 55 further comprising one    or more microbes.-   57. The composition of item 56, wherein the one or more microbes is    selected from the group consisting of Bacillus subtilis, Bacillus    licheniformis, Bacillus amyloliquefaciens, Bacillus cereus, Bacillus    pumilus, Bacillus polymyxa, Bacillus megaterium, Bacillus coagulans,    Bacillus circulans, Bifidobacterium bifidum, Bifidobacterium    animalis, Bifidobacterium sp., Carnobacterium sp., Clostridium    butyricum, Clostridium sp., Enterococcus faecium, Enterococcus sp.,    Lactobacillus sp., Lactobacillus acidophilus, Lactobacillus    farciminus, Lactobacillus rhamnosus, Lactobacillus reuteri,    Lactobacillus salivarius, Lactococcus lactis, Lactococcus sp.,    Leuconostoc sp., Megasphaera elsdenii, Megasphaera sp., Pediococsus    acidilactici, Pediococcus sp., Propionibacterium thoenii,    Propionibacterium sp. and Streptococcus sp. or any combination    thereof.-   58. The composition of any of items 51 to 57 further comprising    plant based material from the sub-family Panicoideae.-   59. The composition of item 58, wherein the plant based material    from the sub-family Panicoideae is maize, corn, sorghum,    switchgrass, millet, pearl millet, foxtail millet or in a processed    form such as milled corn, milled maize, defatted maize, defatted    destarched maize, milled sorghum, milled switchgrass, milled millet,    milled foxtail millet, milled pearl millet, or any combination    thereof.-   60. The composition of any of items 58 to 59, wherein the plant    based material from the sub-family Panicoideae is from the seed    fraction (such as endosperm and/or husk) of the plant.-   61. An animal feed additive comprising the composition of any of    items 51 to 57 and one or more components selected from the list    consisting of:    -   one or more vitamins;    -   one or more minerals;    -   one or more amino acids; and    -   one or more other feed ingredients.-   62. An animal feed comprising the composition of any of items 51 to    60 or the animal feed additive of item 61 and plant based material    from the sub-family Panicoideae.-   63. The animal feed of item 62, wherein the plant based material    from the sub-family Panicoideae is maize, corn, sorghum,    switchgrass, millet, pearl millet, foxtail millet or in a processed    form such as milled corn, milled maize, defatted maize, defatted    destarched maize, milled sorghum, milled switchgrass, milled millet,    milled foxtail millet, milled pearl millet, or any combination    thereof.-   64. The animal feed of any of items 62 to 63, wherein the plant    based material from the sub-family Panicoideae is from the seed    fraction (such as endosperm and/or husk) of the plant.-   65. A polynucleotide encoding the polypeptide of any of items 23 to    24 or 49 to 50.-   66. A nucleic acid construct or expression vector comprising the    polynucleotide of item 65 operably linked to one or more control    sequences that direct the production of the polypeptide in an    expression host.-   67. A recombinant host cell comprising the polynucleotide of item 65    operably linked to one or more control sequences that direct the    production of the polypeptide.-   68. A method of producing the polypeptide of any of items 23 to 24    or 49 to 50, comprising:    -   (a) cultivating a cell, which in its wild-type form produces the        polypeptide, under conditions conductive for production of the        polypeptide; and    -   (b) recovering the polypeptide.-   69. A method of producing the polypeptide of any of items 23 to 24    or 49 to 50, comprising:    -   (a) cultivating the recombinant host cell of item 67 under        conditions conducive for production of the polypeptide; and    -   (b) recovering the polypeptide.-   70. A transgenic plant, plant part or plant cell transformed with a    polynucleotide encoding the polypeptide of any of items 23 to 24 or    49 to 50.-   71. A whole broth formulation or cell culture composition comprising    a polypeptide of any of items 23 to 24 or 49 to 50.

The present invention is further described by the following examplesthat should not be construed as limiting the scope of the invention.

EXAMPLES

Strains

The sources of the strains are listed in table S1.

Genome sequencing, the subsequent assembly of reads and the genediscovery (i.e. annotation of gene functions) is known to the personskilled in the art and the service can be purchased commercially.

TABLE S1 Isolation of strains SEQ ID NO of gene/ Strain Source CountryYear Collection polypeptide Penicillium Ground Pakistan 1962 CBS 292.627/8 capsulatum germlings Penicillium Maize Pretoria, On or CBS 228.9010/11 polonicum (formally South before 1990 P. aurantiogriseum) AfricaAspergillus clavatus Not reported Not On or NRRL 1 13/14 reported before1965 CBS 513.65 40/41 Neosartorya fischeri Canned fruit Not 1923 NRRL18116/17 (apples) reported CBS 544.65 157/158 Ustilago maydis Corn stem USAOn or FGSC9021 19/20 before 1961 175/176 Penicillium oxalicum Soilsample Beijing, 2006 22/23 China Talaromyces Soil sample Yunnan, 200025/26 pinophilus China Streptomyces Garden soil Japan 1952 ATCC 1276928/29 nitrosporeus sample DSM 40023 Aspergillus wentii Soybeans Java Onor CBS104.07 46/47 before 1907 Acrophialophora Forest soil Patharia 1955CBS380.55 52/53 fusispora Forest, ATCC 22556 64/65 IndiaStreptosporangium Soil sample India On or 58/59 sp-60756 before 1993Lasiodiplodia Soil sample Yunnan, 1990 97/98 theobromae China AscobolusDeer dung Denmark On or 100/101 stictoideus A4-1 before 1991 Drechslerasp. Soil sample Egypt On or 103/104 before 1994 Xylanibacterium sp-Environmental United 1990 106/107 61981 sample Kingdom Microdochiumnivale India 1996 112/113 Humicola Soil sample Jordan On or CBS 454.80118/119 hyalothermophila before 1980 Curvularia Setaria italica USA Onor CBS 332.64 121/122 geniculate before 1964 Glycomyces Soil sampleChina 1985 DSM 43812 124/125 rutgersensis Coprinopsis cinereaEnvironmental Japan 1991 FGSC9003 130/131 sample Aspergillus Wood of NotOn or CBS 101.43 136/137 aculeatus Santalum sp. disclosed before 1943DSM 2344 Remersonia Mushroom Switzerland 1962 CBS540.69 139/140thermophila compost Penicillium soppii Leaf sample Sweden 1994 145/146Bipolaris Stem of a Ethiopia On or IMI 325070 148/149 sorokinianaTriticale plant before 1988 Aspergillus Soil sample USA 1989 CBS 117186154/155 fumigatiaffinis Thielavia arenaria Desert soil Egypt On or CBS508.74 160/161 before 1974 Chaetomium Garden soil India 1996 CBS 102434163/164 olivicolor Thielavia terricola Winter pea Not On or CBS 540.50166/167 plans reported before 1950 169/170 Humicola sp. Soil sampleEgypt On or 172/173 before 1993

The origin of the GH11 xylanase from Geobacillus stearothermophilus (SEQID NO: 76) was not reported in ‘Nucleotide sequence analysis of anendo-xylanase gene (xynA) from Bacillus stearothermophilus’, J.Microbiol Biotechnol. 1995 5:117-124.

Preparation of Substrates

Preparation of Destarched Maize (DSM)

107 kg of milled maize (<10 mm) was mixed in a tank with 253 kg of tapwater at 53° C. to make a slurry. The temperature of the slurry was 47°C. and the pH 5.9. The pH was adjusted to 6.15 with 1 L of 1 N NaOH andthe tank was then heated to 95° C. 1.119 kg of Termamyl® alpha-amylase(Novozymes A/S, Bagsvaerd, Denmark) was added at 52° C. and incubatedfor 80 minutes at 95° C. The pH measured at the end of the incubationwas 6.17. Cold tap water was added to the slurry and the slurry wascentrifuged and decanted 3 times using a Westfalia decanter CA-225-110(4950±10 rpm, flow ˜600 l/h) giving 64.5 kg of sludge. The sludge wasthen collected, frozen and freeze-dried to give 17.1 kg of destarchedmaize (DSM).

Preparation of Defatted Destarched Maize (DFDSM)

500 mL acetone was added to 100 gram of destarched maize, prepared asdescribed above. The slurry was stirred for 5 minutes and allowed tosettle. The acetone was decanted and the procedure was repeated 2 times.The residue was air dried overnight to give defatted destarched maize(DFDSM) which was stored at room temperature.

Preparation of Destarched Sorghum

Whole sorghum seeds were milled and sieved and a fraction below 0.5 mmwas used for further processing. The sieved fraction was suspended in 25mM NaOAc pH 5.5 at 20% dry matter and destarched. The destarchinginvolved a first step at 85° C. with 500 ppm Termamyl SC alpha-amylase(Novozymes A/S, Bagsvaerd, Denmark) for 20 min followed by an overnightincubation using 250 ppm Attenuzyme Flex (Novozymes A/S, Bagsvaerd,Denmark) at 65° C. The slurry was centrifuged and the liquid decanted.After this another destarching was made using by adding MilliQ water and200 ppm Termamyl SC and 200 ppm Attenuzyme Flex and incubating overnightat 65° C.

The sorghum fiber was separated from the liquid by vacuum filtrationthrough a Whatman F glass fiber filter. The filter cake was then washedseveral times with excess of water to remove soluble sugars. Finally thedestarched sorghum fiber was dried in an oven at 65° C. and the dryfiber milled quickly in a coffee grinder so that the particle size wasin general less than 1 mm.

Assays

Xylose Assay

A xylose standard curve from 0 to 125 μg xylose/mL was prepared from astock solution of 2.5 mg xylose/mL (prepared by dissolving 0.125 gxylose in 50 mL de-ionised water).

Assay principle. The interconversion of the α- and β-anomeric forms ofD-xylose is catalysed by xylose mutarotase (XMR) using the D-xyloseassay kit from Megazyme International Ireland. The β-D-xylose isoxidised by NAD+ to D-xylonic acid in the presence of β-xylosedehydrogenase (β-XDH) at pH 7.5. The amount of NADH formed in thisreaction is stoichiometric with the amount of D-xylose and is measuredby the increase in absorbance at 340 nm.

Example 1: GH62 Arabinofuranosidase from Penicillium capsulatum (SEQ IDNO: 9)

The GH62 arabinofuranosidase from Penicillium capsulatum (SEQ ID NO: 9)was cloned, expressed and purified as described in WO2006/125438.

Example 2: Cloning of GH62 Arabinofuranosidase from Penicilliumaurantiogriseum (SEQ ID NO: 12)

The arabinofuranosidase with nucleotide sequence SEQ ID NO: 10 was PCRamplified from genomic DNA isolated from Penicillium aurantiogriseum andcloned into the expression vector pDAu222 using BamHI and HindIIIrestriction sites as described in WO 2013024021.

The final expression plasmids were individually transformed into theAspergillus oryzae Bech2 expression host. Host organism Aspergillusoryzae BECh2 is described in WO 00/39322. It is a mutant of JaL228(described in WO98/123000), which is a mutant of IF04177. Thearabinofuranosidase genes were integrated by ectopic integration intothe A. oryzae bech2 host cell genome upon transformation.

The gene coding for amdS was used as marker. Transformants were selectedon sucrose media agar supplemented with 10 mM acetamide. For productionof the recombinant arabinofuranosidase, a single Aspergillustransformant was cultured in 18 500 ml baffled flasks each containing150 ml of DAP-4C-1 medium (WO 12/103350). The cultures were shaken on arotary table at 200 RPM at 30° C. for 3 days. The culture brothsubsequently was separated from cellular material by filtration througha stack of filters with 1.6, 1.2, and 0.7 um pore sizes, followed bypassage through a 0.45 um filter.

Example 3: Purification of GH62 Arabinofuranosidase from Penicilliumaurantiogriseum (SEQ ID NO: 12)

The filtrated broth from example 2 was adjusted to pH8.0 and filtratedon 0.22 μm PES filter (Nalge Nunc International, Nalgene labware cat#595-4520). The filtrate was loaded onto a MEP Hypercel™ column (PallCorporation, Long Island, N.Y., USA) equilibrated with 50 mM TRIS pH8.0.After wash with equilibration buffer, the bound proteins were batcheluted with 50 mM acetic acid pH 4.5. Fractions were collected andanalyzed by SDS-PAGE. The fractions were applied to a SP SEPHAROSE® FastFlow column (GE Healthcare, Piscataway, N.J., USA) equilibrated with 50mM acetic acid pH 4.5 and bound proteins were eluted with a lineargradient from 0-1000 mM sodium chloride over 20 CV. Fractions werecollected and analyzed by SDS-PAGE.

Example 4: Cloning of GH62 Arabinofuranosidases from Aspergillusclavatus (SEQ ID NO: 15), Neosartorya fischeri (SEQ ID NO: 18) andUstilago maydis (SEQ ID NO: 21)

The wild type genes from Aspergillus clavatus (Uniprot:XM_001273614),Neosartorya fischeri (Uniprot:XM_001265651) and Ustilago maydis(Uniprot:XM_755363) were codon optimized for Aspergillus oryzae givingnucleotide sequences SEQ ID NO: 13, SEQ ID NO: 16 and SEQ ID NO: 19respectively which were synthesized and purchased commercially (Geneartand Lifetechnologies). E. coli DH10B competent cells were transformedwith a construct including the gene as described above forre-constitution and maintenance.

The final expression plasmids were individually transformed into theAspergillus oryzae MT3568 expression host. A. oryzae MT3568 is aderivative of A. oryzae JaL355 (WO02/40694) in which pyrG auxotrophy wasrestored by disrupting the A. oryzae acetamidase (amdS) gene with thepyrG gene. The arabinofuranosidase genes were integrated by homologousrecombination into the A. oryzae MT3568 host cell genome upontransformation.

The gene coding for amdS was used as marker. Transformants were selectedon sucrose agar plate supplemented with 10 mM acetamide. One recombinantAspergillus oryzae clone containing the respective arabinofuranosidaseexpression construct was selected and was cultivated on a rotary shakerin 3* 1-liter baffled conical flasks each containing 300 ml DAP4C-1(DAP4C-1 medium was composed of 11 g of MgSO₄.7H₂O, 1 g KH₂PO₄, 2 g ofcitric acid, monohydrate, 20 g of dextrose, 10 g of maltose, 6 g ofK₃PO₄.3H₂O, 0.5 g of yeast extract, 0.5 ml of trace metals solution, anddeionized water to 1 liter. The medium was portioned out to flasks,adding 1 gram CaCO₃ to each 300 ml portion. The medium was sterilized inan autoclave. After cooling the following was added to 300 ml of medium:7 ml of filter sterilized 50% w/v (NH₄)₂HPO₄, and 10 ml of filtersterilized 20% lactic acid). After 3 days cultivation time at 30° C.,180 rpm enzyme containing supernatants were harvested by filtrationusing a 0.22 μm 1-liter bottle (Borosil) top vacuum filter (GEHealthcare).

Example 5: Purification of GH62 Arabinofuranosidases from Aspergillusclavatus (SEQ ID NO: 15), Neosartorya fischeri (SEQ ID NO: 18) andUstilago maydis (SEQ ID NO: 21)

The filtrate from example 4 was pH adjusted to pH 7, loaded onto aToyopearl Phenyl-650 resin column (Tosoh Bioscience) and equilibratedwith equilibration buffer (ammonium sulfate (1.5M)+HEPES (50 mM, pH 7)).After washing with equilibration buffer, the bound proteins were batcheluted with 0.9M Ammonium Sulphate in HEPES (50 mM, pH 7). Fractionswere collected and analyzed by SDS-PAGE. Fractions containing a band atapproximately 41 kDa (SEQ ID NO: 15 and SEQ ID NO: 18) or 34 kDa (SEQ IDNO: 21) were pooled. The sample was buffer exchanged with HEPES (50 mM,pH 7) and concentrated using a Quixstand fitted with a 10 KDa cutoffmembrane.

Example 6: Cloning of GH62 Arabinofuranosidases from Penicilliumoxalicum (SEQ ID NO: 24) and Talaromyces pinophilus (SEQ ID NO: 27)

The arabinofuranosidases with nucleotide sequences SEQ ID NO: 22 and SEQID NO: 25 were PCR amplified from genomic DNA isolated from Penicilliumoxalicum and Talaromycespinophilus respectively and cloned into theexpression vector pCaHj505 as described in WO2013029496.

The final expression plasmids were individually transformed into theAspergillus oryzae MT3568 expression host. A. oryzae oryzae MT3568 is aderivative of A. oryzae JaL355 (WO02/40694) in which pyrG auxotrophy wasrestored by disrupting the A. oryzae acetamidase (amdS) gene with thepyrG gene. The arabinofuranosidase genes were integrated by homologousrecombination into the A. oryzae MT3568 host cell genome upontransformation.

The gene coding for amdS was used as marker. Transformants were selectedon pyrG media agar supplemented with 10 mM acetamide. One recombinantAspergillus oryzae clone containing the respective arabinofuranosidaseexpression construct was selected and was cultivated on a rotary shakingtable in 4 2-liter baffled Erlenmeyer flasks each containing 400 ml YPM(1% Yeast extract, 2% Peptone and 2% Maltose). After 3 days cultivationtime at 30° C., enzyme containing supernatants were harvested byfiltration using a 0.22 μm 1-liter bottle top vacuum filter (CorningInc., Corning, N.Y., USA).

Example 7: Purification of GH62 Arabinofuranosidases from Penicilliumoxalicum (SEQ ID NO: 24) and Talaromyces pinophilus (SEQ ID NO: 27)

A 1600 ml volume of filtered supernatant of Aspergillus oryzae fromexample 6 was precipitated with ammonium sulfate (80% saturation),re-dissolved in 50 ml of 20 mM NaOAc pH 5.5, dialyzed against the samebuffer, and filtered through a 0.45 μm filter. The final volume was 60ml. The solution was applied to a 40 ml Q SEPHAROSE® Fast Flow column(GE Healthcare, Buckinghamshire, UK) equilibrated with 20 mM NaOAc pH5.5. Proteins were eluted with a linear 0-0.25 M NaCl gradient.Fractions were analyzed by SDS-PAGE using a NUPAGE® NOVEX® 4-12%Bis-Tris Gel with 50 mM MES. The resulting gel was stained withINSTANTBLUE™. Fractions containing a band at approximately 33 kDa werepooled. Then the pooled solution was concentrated by ultrafiltration.

Example 8: Cloning of GH62 Arabinofuranosidase from Streptomycesnitrosporeus (SEQ ID NO: 33), Streptomyces beijiangensis (SEQ ID NO: 39)and Streptosporangium sp-60756 (SEQ ID NO: 63)

Bacterial GH62 sequences were cloned from Streptomyces nitrosporeus (SEQID NO: 28), Streptomyces beijiangensis (SEQ ID NO: 34) andStreptosporangium sp-60756 (SEQ ID NO: 58).

The AraFs were cloned into a Bacillus expression vector as described inWO 12/025577. The DNA encoding the mature AraF peptide were cloned inframe to a Bacillus clausii secretion signal (BcSP; with the followingamino acid sequence: MKKPLGKIVASTALLISVAFSSSIASA (SEQ ID NO: 90)). BcSPreplaced all native secretion signals respectively in all genes.

Downstream of the BcSP sequence an affinity tag sequence was introducedto ease the purification process (His-tag; with the following amino acidsequence: HHHHHHPR (SEQ ID NO: 92) The gene that was expressed thereforecomprised the BcSP sequence followed by the His-tag sequence followed bythe mature wild type AraF sequence (as shown in SEQ ID NO: 31, SEQ IDNO: 37 and SEQ ID NO: 61 respectively).

The final expression plasmids (BcSP-His-tag-GH62) were individuallytransformed into a Bacillus subtilis expression host. The AraFBcSP-fusion genes were integrated by homologous recombination into theBacillus subtilis host cell genome upon transformation.

The gene construct was expressed under the control of a triple promotersystem (as described in WO 99/43835). The gene coding forchloramphenicol acetyltransferase was used as maker (as described in(Diderichsen et al., 1993, Plasmid 30: 312-315)). Transformants wereselected on LB media agar supplemented with 6 microgram ofchloramphenicol per ml. One recombinant Bacillus subtilis clonecontaining the respective arabinofuranosidase expression construct wasselected and was cultivated on a rotary shaking table in 500 ml baffledErlenmeyer flasks each containing 100 ml yeast extract-based media.After 3-5 days cultivation time at 30° C. to 37° C., enzyme containingsupernatants were harvested by centrifugation and the enzymes werepurified by His-tag purification.

Example 9: Purification of GH62 Arabinofuranosidase from Streptomycesnitrosporeus (SEQ ID NO: 33), Streptomyces beijiangensis (SEQ ID NO: 39)and Streptosporangium sp-60756 (SEQ ID NO: 63)

The His-tagged enzymes from example 8 were purified by immobilized metalchromatography (IMAC) using Ni2+ as the metal ion on 5 mL HisTrap Excelcolumns (GE Healthcare Life Sciences). The purification took place at pH8 and the bound proteins were eluted with imidazole. The purity of thepurified enzymes was checked by SDS-PAGE and the concentration of eachenzyme determined by Abs 280 nm after a buffer exchange.

Example 10: Cloning of GH62 Arabinofuranosidase from Aspergillusclavatus (SEQ ID NO: 45)

The arabinofuranosidase with nucleotide sequence SEQ ID NO: 40 was PCRamplified from genomic DNA isolated from Aspergillus clavatus and clonedinto the Aspergillus expression vector pMStr366. The vector pMStr366 isa version of the expression vector pMStr57 (WO 04/032648) that has beenmodified to allow fusion of an insert CDS to a vector-encoded HIS tagwith the sequence RHHHHHHP (SEQ ID NO: 91). The nucleotide sequence ofthe resulting fusion is shown in SEQ ID NO: 43 and the peptidetranslation of the His-tagged protein is shown in SEQ ID NO: 44.

The sequence of the tagged arabinofuranosidase encoding gene cloned inthe expression vector was confirmed and the expression construct wastransformed into the Aspergillus oryzae strain MT3568 (WO 11/057140).Transformants were selected on acetamide during regeneration fromprotoplasts and subsequently re-isolated under selection (Christensen etal., 1988, Biotechnology 6, 1419-1422 and WO 04/032648).

For production of the recombinant arabinofuranosidase, a singleAspergillus transformant was cultured in two 500 ml baffled flasks eachcontaining 150 ml of DAP-4C-1 medium (WO 12/103350). The cultures wereshaken on a rotary table at 150 RPM at 30° C. for 3 days. The culturebroth subsequently was separated from cellular material by passagethrough a 0.22 um filter.

Example 11: Purification of the Arabinofuranosidase from Aspergillusclavatus (SEQ ID NO: 45)

The pH of the filtrated sample from example 10 was adjusted to around pH7.5 and 1.8M ammonium sulfate was added. The sample was applied to a 5ml HiTrap™ Phenyl (HS) column on an Akta Explorer. Prior to loading, thecolumn had been equilibrated in 5 column volumes (CV) of 50 mMHEPES+1.8M ammonium sulfate pH 7. In order to remove unbound material,the column was washed with 5 CV of 50 mM HEPES+1.8M ammonium sulfate pH7. The target protein was eluted from the column into a 10 ml loop using50 mM HEPES+20% isopropanol pH 7. From the loop, the sample was loadedonto a desalting column (HiPrep™ 26/10 Desalting), which had beenequilibrated with 3CV of 50 mM HEPES+100 mM NaCl pH 7.0. The targetprotein was eluted with 50 mM HEPES+100 mM NaCl pH 7.0 and relevantfractions were selected and pooled based on the chromatogram. The flowrate was 5 ml/min.

Example 12: Cloning of GH62 Arabinofuranosidase from Aspergillus wentii(SEQ ID NO: 51)

The arabinofuranosidase with nucleotide sequence SEQ ID NO: 46 was PCRamplified from genomic DNA isolated from Aspergillus wentii and clonedinto the expression vector pDAu222 as described in WO 2013024021 usingBamHI and MluI restriction sites to create a C-terminal His-tag fusionconstruct with the nucleotide sequence shown in SEQ ID NO: 49 and thepeptide translation of the His-tagged protein shown in SEQ ID NO: 50.

The sequence of the tagged arabinofuranosidase encoding gene cloned inthe expression vector was confirmed and the expression construct wastransformed into the Aspergillus oryzae strain MT3568 (WO 11/057140).Transformants were selected on acetamide during regeneration fromprotoplasts and subsequently re-isolated under selection (Christensen etal., 1988, Biotechnology 6, 1419-1422 and WO 04/032648).

For production of the recombinant arabinofuranosidase, a singleAspergillus transformant was cultured in two 500 ml baffled flasks eachcontaining 150 ml of DAP-4C-1 medium (WO 12/103350). The cultures wereshaken on a rotary table at 150 RPM at 30° C. for 3 days. The culturebroth subsequently was separated from cellular material by passagethrough a 0.22 um filter.

Example 13: Purification of GH62 Arabinofuranosidase from Aspergilluswentii (SEQ ID NO: 51)

The filtrated broth from example 12 was adjusted to pH8.0 and filtratedon 0.22 μm PES filter (Nalge Nunc International, Nalgene labware cat#595-4520). The filtrate was loaded onto a MEP Hypercel™ column (PallCorporation, Long Island, N.Y., USA) equilibrated with 50 mM TRIS pH8.0.After wash with equilibration buffer, the bound proteins were batcheluted with 50 mM acetic acid pH 4.5. Fractions were collected andanalyzed by SDS-PAGE. The fractions were applied to a SP SEPHAROSE® FastFlow column (GE Healthcare, Piscataway, N.J., USA) equilibrated with 50mM acetic acid pH 4.5 and bound proteins were eluted with a lineargradient from 0-1000 mM sodium chloride over 20 CV. Fractions werecollected and analyzed by SDS-PAGE.

Example 14: Cloning of GH62 Arabinofuranosidase from Acrophialophorafusispora (SEQ ID NO: 57)

The arabinofuranosidase with nucleotide sequence SEQ ID NO: 52 was PCRamplified from genomic DNA isolated from Acrophialophora fusispora andcloned into the expression vector pDAu222 as described in WO 2013024021using BamHI and MluI restriction sites to create a C-terminal His-tagfusion construct with the nucleotide sequence shown in SEQ ID NO: 55 andthe peptide translation of the His-tagged protein shown in SEQ ID NO:56.

The sequence of the tagged arabinofuranosidase encoding gene cloned inthe expression vector was confirmed and the expression construct wastransformed into the Aspergillus oryzae strain MT3568 (WO 11/057140).Transformants were selected on acetamide during regeneration fromprotoplasts and subsequently re-isolated under selection (Christensen etal., 1988, Biotechnology 6, 1419-1422 and WO 04/032648).

For production of the recombinant arabinofuranosidase, a singleAspergillus transformant was cultured in two 500 ml baffled flasks eachcontaining 150 ml of DAP-4C-1 medium (WO 12/103350). The cultures wereshaken on a rotary table at 150 RPM at 30° C. for 3 days. The culturebroth subsequently was separated from cellular material by passagethrough a 0.22 um filter.

Example 15: Purification of GH62 Arabinofuranosidase fromAcrophialophora fusispora (SEQ ID NO: 57)

The filtrated broth from example 14 was adjusted to pH8.0 and filtratedon 0.22 μm PES filter (Nalge Nunc International, Nalgene labware cat#595-4520). The filtrate was loaded onto a MEP Hypercel™ column (PallCorporation, Long Island, N.Y., USA) equilibrated with 50 mM TRIS pH8.0.After wash with equilibration buffer, the bound proteins were batcheluted with 50 mM acetic acid pH 4.5. Fractions were collected andanalyzed by SDS-PAGE. The fractions were applied to a SP SEPHAROSE® FastFlow column (GE Healthcare, Piscataway, N.J., USA) equilibrated with 50mM acetic acid pH 4.5 and bound proteins were eluted with a lineargradient from 0-1000 mM sodium chloride over 20 CV. Fractions werecollected and analyzed by SDS-PAGE.

Example 16: Cloning of GH62 Arabinofuranosidase from Acrophialophorafusispora (SEQ ID NO: 69)

The arabinofuranosidase with nucleotide sequence SEQ ID NO: 64 was PCRamplified from genomic DNA isolated from Acrophialophora fusispora andcloned into the expression vector pDAu222 as described in WO 2013024021using BamHI and MluI restriction sites to create a C-terminal His-tagfusion construct with the nucleotide sequence shown in SEQ ID NO: 67 andthe peptide translation of the His-tagged protein shown in SEQ ID NO:68.

The sequence of the tagged arabinofuranosidase encoding gene cloned inthe expression vector was confirmed and the expression construct wastransformed into the Aspergillus oryzae strain MT3568 (WO 11/057140).Transformants were selected on acetamide during regeneration fromprotoplasts and subsequently re-isolated under selection (Christensen etal., 1988, Biotechnology 6, 1419-1422 and WO 04/032648).

For production of the recombinant arabinofuranosidase, a singleAspergillus transformant was cultured in two 500 ml baffled flasks eachcontaining 150 ml of DAP-4C-1 medium (WO 12/103350). The cultures wereshaken on a rotary table at 150 RPM at 30° C. for 3 days. The culturebroth subsequently was separated from cellular material by passagethrough a 0.22 um filter.

Example 17: Purification of GH62 Arabinofuranosidase fromAcrophialophora fusispora (SEQ ID NO: 69)

The filtrated broth from example 16 was adjusted to pH8.0 and filtratedon 0.22 μm PES filter (Nalge Nunc International, Nalgene labware cat#595-4520). The filtrate was loaded onto a MEP Hypercel™ column (PallCorporation, Long Island, N.Y., USA) equilibrated with 50 mM TRIS pH8.0.After wash with equilibration buffer, the bound proteins were batcheluted with 50 mM acetic acid pH 4.5. Fractions were collected andanalyzed by SDS-PAGE. The fractions were applied to a SP SEPHAROSE® FastFlow column (GE Healthcare, Piscataway, N.J., USA) equilibrated with 50mM acetic acid pH 4.5 and bound proteins were eluted with a lineargradient from 0-1000 mM sodium chloride over 20 CV. Fractions werecollected and analyzed by SDS-PAGE.

Example 18: Cloning of the GH11 Xylanase 1 from Geobacillusstearothermophilus (SEQ ID NO: 81)

The GH11 xylanase 1 gene from Geobacillus stearothermophilus has beenpublished by Cho, S and Choi, Y (Nucleotide sequence analysis of anendo-xylanase gene (xynA) from Bacillus stearothermophilus, J MicrobiolBiotechnol. 1995 5:117-124 (UNIPROT:P45705)). The gene encoding the GH11xylanase 1 from Geobacillus stearothermophilus was cloned as a codonoptimised synthetic gene based on the published nucleotide sequence (SEQID NO: 76). The synthetic gene having SEQ ID NO: 79, was synthesized bythe company DNA2.0 (Headquarter, 1430 O'Brien Drive, Suite E, MenloPark, Calif. 94025, USA). The synthetic gene was delivered as a clonedfragment in their standard cloning vector. A linear integrationvector-system was used for the expression cloning of the GH11 xylanase 1from Geobacillus stearothermophilus. The linear integration constructwas a PCR fusion product made by fusion of the gene between two Bacillussubtilis homologous chromosomal regions along with a strong promoter anda chloramphenicol resistance marker. The fusion was made by SOE PCR(Horton, R. M., Hunt, H. D., Ho, S. N., Pullen, J. K. and Pease, L. R.(1989) Engineering hybrid genes without the use of restriction enzymes,gene splicing by overlap extension Gene 77: 61-68). The SOE PCR methodis also described in patent application WO 2003095658. The gene wasexpressed under the control of a triple promoter system (as described inWO 99/43835), consisting of the promoters from Bacillus licheniformisalpha-amylase gene (amyL), Bacillus amyloliquefaciens alpha-amylase gene(amyQ), and the Bacillus thuringiensis cryIIIA promoter includingstabilizing sequence. The gene coding for chloramphenicolacetyl-transferase was used as marker (described in e.g. Diderichsen,B.; Poulsen, G. B.; Joergensen, S. T.; A useful cloning vector forBacillus subtilis. Plasmid 30:312 (1993)). The final gene constructswere integrated on the Bacillus chromosome by homologous recombinationinto the pectate lyase locus. The gene was amplified by PCR from theplasmid delivered by the company DNA2.0 with gene specific primerscontaining overhang to the two flanking fragments. The upstream anddownstream flanking fragments were amplified from genomic DNA of thestrain iMB1361 (described in patent application WO 2003095658). The GH11xylanase 1 was expressed with a Bacillus lentus secretion signal (withthe following amino acid sequence: MKKPLGKIVASTALLISVAFSSSIASA (SEQ IDNO: 90)) replacing the native secretion signal. The resulting expressedgene sequence is SEQ ID NO: 79. The 2 linear vector fragments and thegene fragment was subjected to a Splicing by Overlap Extension (SOE) PCRreaction to assemble the 3 fragments into one linear vector construct.An aliquot of the PCR product was transformed into Bacillus subtilis.Transformants were selected on LB plates supplemented with 6 μg ofchloramphenicol per ml. A recombinant Bacillus subtilis clone containingthe integrated expression construct was grown in liquid culture. Theenzyme containing supernatant was harvested and the enzyme purified asdescribed in example 19.

Example 19: Purification of the GH11 Xylanase 1 from Geobacillusstearothermophilus (SEQ ID NO: 81)

Filtrated broth was adjusted to pH8.0 and filtrated on 0.22 μm PESfilter (Nalge Nunc International, Nalgene labware cat #595-4520). Thefiltrate was loaded onto a MEP Hypercel™ column (Pall Corporation, LongIsland, N.Y., USA) equilibrated with 50 mM TRIS pH8.0. After wash withequilibration buffer, the bound proteins were batch eluted with 100 mMacetic acid pH 4.5. Fractions were collected and analyzed by SDS-PAGE.The fractions were pooled and applied to a Sephadex™ G-25 (medium) (GEHealthcare, Piscataway, N.J., USA) column equilibrated in 20 mM MES pH6.0. The fractions were then applied to a SP SEPHAROSE® Fast Flow column(GE Healthcare, Piscataway, N.J., USA) equilibrated with 20 mM MES pH6.0 and bound proteins were eluted with a linear gradient from 0-1000 mMsodium chloride over 20 CV. Fractions were collected and analyzed bySDS-PAGE.

Example 20: Cloning of the GH11 Xylanase from Streptomyces beijiangensis(SEQ ID NO: 87)

Bacterial xylanase sequence was cloned from Streptomyces beijiangensis(SEQ ID NO: 82). The xylanase was cloned into a Bacillus expressionvector as described in WO 12/025577. The DNA encoding the maturexylanase peptide was cloned in frame to a Bacillus clausii secretionsignal (BcSP; with the following amino acid sequence:MKKPLGKIVASTALLISVAFSSSIASA (SEQ ID NO: 90), originating from theprotease AprH of B. clausii). BcSP replaced the native secretion signal.

Downstream of the BcSP sequence an affinity tag sequence was introduced(His-tag; with the following amino acid sequence: HHHHHHPR (SEQ ID NO:92). The gene that was expressed therefore comprised the BcSP sequencefollowed by the His-tag sequence followed by the mature wild typexylanase sequence (as shown in SEQ ID NO: 85).

The final expression plasmid (BcSP-His-tag-GH11) was transformed into aBacillus subtilis expression host. The Xyl BcSP-fusion genes wereintegrated by homologous recombination into the Bacillus subtilis hostcell genome upon transformation.

The gene construct was expressed under the control of a triple promotersystem (as described in WO 99/43835). The gene coding forchloramphenicol acetyltransferase was used as maker (as described in(Diderichsen et al., 1993, Plasmid 30: 312-315)). Transformants wereselected on LB media agar supplemented with 6 microgram ofchloramphenicol per ml. One recombinant Bacillus subtilis clonecontaining the respective xylanase expression construct was selected andwas cultivated on a rotary shaking table in 500 ml baffled Erlenmeyerflasks each containing 100 ml yeast extract-based media. After 3-5 dayscultivation time at 30° C. to 37° C., enzyme containing supernatantswere harvested by centrifugation and the enzyme purified as described inexample 21.

Example 21: Purification of the GH11 Xylanase from Streptomycesbeijiangensis (SEQ ID NO: 87)

Filtrated broth was applied to a Sephadex™ G-25 (medium) (GE Healthcare,Piscataway, N.J., USA) column equilibrated in 100 mM sodium acetate pH5.0, 5 mM CaCl₂. The fractions were pooled and added an equal volume of9 g/L NaCl in MQ-water. Each sample was then concentrated 6 times usinga using a Vivaspin 20 centrifugal concentrator with a 10,000 MWCO PESmembrane (Sartorius Stedim Biotech GmbH, 37070 Goettingen, Germany).Protein concentration was determined using SDS-PAGE analysis.

Example 22: Measurement of Soluble and Insoluble Dietary Fiber in theSubstrate Defatted De-Starched Maize (DFDSM) and Correlation to SolubleXylose Measured after Enzymatic Incubation

400 mg of defatted de-starched maize (DFDSM) was added to NaOAc-buffer(5 mL, pH 5). The mixture was heated to between 90-100° C., thenTermamyl 300 DX (100 μL, Novozymes A/S, Bagsvaerd, Denmark) was addedand the mixture was incubated for 1 hr. The mixture was then cooled andamyloglucosidase from Aspergillus niger (500 μL, catalogue numberE-AMGDF, for use in Megazyme Total Starch and Dietary Fiber, MegazymeInternational Ireland, Wicklow, Ireland) was added and samples wereincubated overnight (16 h) at 60° C. The mixture was then cooled andcentrifuged at 2500×g for 10 min at 5° C. The supernatant was collectedand NaOAc-buffer (5 mL, pH 5) was added to the residue and centrifugedat 2500×g, 10 min, 5° C. This procedure was repeated twice. Thesupernatants were then collected, pooled and analysed for soluble NSP asdescribed in A. The residue was analysed for insoluble NSP as describedin B.

A: Soluble NSP, Supernatant

The pooled supernatants were diluted to a fixed volume from which a 5 mLaliquot of supernatant was taken. To this aliquot was added 20.1 mL cold99.9% ethanol and the mixture was kept on ice for approx. 15 min forprecipitation of polymers with a DP>10. After centrifuging at 2500×g, 5°C. for 10 min, the supernatant was discarded.

5 mL cold 80% ethanol was added to the pellet and the mixture was kepton ice for approx. 15 min. After centrifuging at 2500×g, 5° C. for 10min, the supernatant was discarded.

Acid hydrolysis of the precipitate was conducted by the addition of MQwater (7.9 mL), myoinositol (0.5 mL, internal standard) and 12M H₂SO₄(0.3 mL) and autoclaving at 125° C. for 55 minutes.

B: Insoluble NSP, Residue

The pellet obtained after AMG treatment was hydrolysed by the additionof MQ water (74 mL), myoinositol (10 mL, internal standard) and 12MH₂SO₄ (3 mL) and autoclaving at 125° C. for 55 minutes.

C. GLC Analysis

After autoclaving, the samples were reduced with borohydride to producealditol sugars and these were derivatised by acetylation to becomevolatile for GLC analyses on an instrument with FID detector (Petterssonet al, (1995) “Total dietary fiber determined as neutral sugar residues,uronic acid residues, and Klason lignin (the Uppsala method),Collaborative study”, J. AOAC Int 78:1030-1044). The concentration ofthe soluble or insoluble sugars was determined relative tomyo-inositiol.

Example 23: Calculation of Percentage Solubilised Xylose

When DFDSM is incubated with enzyme at 40° C. for 4 hours, the enzymesolubilizes the xylan in the substrate and this solubilized xylan isthen hydrolysed further by acid. The xylose released is measuredspectrophotometrically using a D-xylose assay kit (Megazyme, cataloguenumber K-xylose). This xylose (which is actually enzyme solubilizedxylan) is then correlated to the amount of total xylose of the substratemeasured by GLC as described in part C of example 22.

The DFDSM contains 99% insoluble and 1% soluble xylose, in total 14.81%xylose which represents the concentration of xylose polymer (DP>10)present in the sample (DFDSM) according to the analysis. Based on therelease of xylose measured by the Megazyme kit which calculates releasebased on sample weight, the amount of xylose released can be calculatedas follows: e.g. 1% release from 400 mg of sample equals 4 mg of xylose.In 400 mg sample there is 400 mg×14.81% xylose, equal to 59.22 mgxylose. The gross xylose (insoluble+soluble) release is that case 4mg/59.22 mg which represents a release of 6.75% of total xylosepolymers, but it should be noted that this value must be corrected forthe passive release obtained for the non-enzyme supplemented control.This corrected value is defined herein as the percentage solubilisedxylose.

Example 24: Hydrolysis of Defatted Destarched Maize (DFDSM) Using aCombination of a GH10 or 11 Xylanase and GH43 and/or GH51Arabinofuranosidases

Defatted destarched maize (DFDSM, 400 mg) was added to aqueous sodiumacetate (0.1 M, 3.9 mL) solution containing calcium chloride (5 mM) atpH 5 and the mixture heated to 40° C. for 30 minutes. 1004 buffer orenzyme solution was added and the sample was heated at 40° C. for 4hours. The sample was cooled to 5° C. and centrifuged (4000 rpm, 5° C.)for 10 minutes. 1.7 mL of the sample was transferred to an Eppendorftube and the enzyme deactivated by heating to 95° C. for 10 minutes. Thesamples were then frozen until hydrolysed (within 72 hours and xylosedetermination was performed immediately after hydrolysis).

The supernatant was thawed and centrifuged (14000 rpm) for 5 minutes.The supernatant (2504) was diluted with Milli-Q water (250 μL) in glasstubes and HCl (1.63 M, 2.0 mL) was added. The reaction was heated to100° C. for 1 hour then cooled in an ice bath. Aqueous NaOH solution(1.3 M, 2.5 mL) was added whilst the samples were cooled on ice and thesamples were stored at 0-5° C. whilst xylose content was analysed usingthe xylose assay. The results are presented in tables 2, 3 and 4.

TABLE 2 Xylose release from DFDSM using a GH10 or 11 xylanase or a GH43,GH51 or GH62 arabinofuranosidase Conc. Percent GH10 or GH11 [mg Conc.[mg Soluble solubilised Xylanase EP/kg] Arabinofuranosidase EP/kg]xylose (%) xylose¹ None — None — 0 0 Ronozyme WX 200 ppm None — 0.04 0.1SEQ ID NO: 70 10 None — 0.13 0.7 None — SEQ ID NO: 93 10 0.03 0.0 None —SEQ ID NO: 94 10 0.02 0.0 None — SEQ ID NO: 24 10 0.07 0.3 Table 2 showsthe amount of xylose measured after acid hydrolysis of supernatants (%of dry matter and % solubilized xylose of total xylose) when incubatingDFDSM with either a xylanase (Ronozyme WX, a GH11 xylanase fromThermomyces lanuginosus or the GH10 xylanase of SEQ ID NO: 70), the GH43arabinofuranosidase from Humicola insolens as disclosed as SEQ ID NO: 1in WO2006/114095 (SEQ ID NO: 93 herein), the GH51 arabinofuranosidasefrom Meripilus giganteus as disclosed as SEQ ID NO: 2 in WO2006/114095(SEQ ID NO: 94 herein) or a GH62 arabinofuranosidase of the invention(SEQ ID NO: 24). ¹Percentage solubilised xylose was calculated asdescribed in example 23.

TABLE 3 Xylose release from DFDSM using a GH10 xylanase and a GH43, GH51or GH62 arabinofuranosidase Percent Conc. [mg Conc. [mg Solublesolubilised GH10 Xylanase EP/kg] Arabinofuranosidase EP/kg] xylose (%)xylose¹ None — None — 0 0 SEQ ID NO: 70 10 None — 0.15 0.8 SEQ ID NO: 7010 SEQ ID NO: 93 — 0.18 1.1 SEQ ID NO: 70 10 SEQ ID NO: 94 10 0.18 1.1SEQ ID NO: 70 10 SEQ ID NO: 93 + 10 + 10 0.21 1.3 SEQ ID NO: 94 SEQ IDNO: 70 10 SEQ ID NO: 24 10 0.55 3.5 Table 3 shows the amount of xylosemeasured after acid hydrolysis of supernatants (% of dry matter and %solubilized xylose of total xylose) when incubating DFDSM with the GH10xylanase of SEQ ID NO: 70 alone or in combination with the GH43arabinofuranosidase from Humicola insolens as disclosed as SEQ ID NO: 1in WO2006/114095 (SEQ ID NO: 93 herein), the GH51 arabinofuranosidasefrom Meripilus giganteus as disclosed as SEQ ID NO: 2 in WO2006/114095(SEQ ID NO: 94 herein) or both the GH43 and GH51 arabinofuranosidases.For reference a GH62 arabinofuranosidase of the invention (SEQ ID NO:24) was also tested with the GH10 xylanase of SEQ ID NO: 70. ¹Percentagesolubilised xylose was calculated as described in example 23.

TABLE 4 Xylose release from DFDSM using a GH11 xylanase and a GH43, GH51or GH62 arabinofuranosidase Conc. Percent [mg Conc. [mg Solublesolubilised GH11 Xylanase EP/kg] Arabinofuranosidase EP/kg] xylose (%)xylose¹ None — None — 0 0.0 Ronozyme WX 200 ppm None — 0.03 0.1 RonozymeWX 200 ppm SEQ ID NO: 93 — 0.03 0.1 Ronozyme WX 200 ppm SEQ ID NO: 94 100.04 0.2 Ronozyme WX 200 ppm SEQ ID NO: 93 + 10 + 10 0.05 0.3 SEQ ID NO:94 Ronozyme WX 200 ppm SEQ ID NO: 24 10 0.52 3.4 Table 4 shows theamount of xylose measured after acid hydrolysis of supernatants (% ofdry matter and % solubilized xylose of total xylose) when incubatingDFDSM with Ronozyme WX (a GH11 xylanase from Thermomyces lanuginosus)alone or in combination with the GH43 arabinofuranosidase from Humicolainsolens as disclosed as SEQ ID NO: 1 in WO2006/114095 (SEQ ID NO: 93herein), the GH51 arabinofuranosidase from Meripilus giganteus asdisclosed as SEQ ID NO: 2 in WO2006/114095 (SEQ ID NO: 94 herein) orboth the GH43 and GH51 arabinofuranosidases. For reference a GH62arabinofuranosidase of the invention (SEQ ID NO: 24) was also testedwith Ronozyme WX. ¹Percentage solubilised xylose was calculated asdescribed in example 23.Conclusion

The results show that the percent solubilised xylose is notsignificantly higher for the combination of a GH10 or GH11 xylanase andthe prior art GH43 or GH51 arabinofuranosidases compared to the GH10 orGH11 xylanase alone. Further, the percent solubilised xylose for thecombination of a GH10 or GH11 xylanase, the prior art GH43arabinofuranosidases (which has activity towards di-substituted xyloses)and the prior art GH51 arabinofuranosidases (which has activity towardsC2- or C3-position mono-substituted xyloses) is also not significantlyhigher compared to the GH10 or GH11 xylanase alone.

In comparison, the combination of a GH10 or GH11 xylanase and SEQ ID NO:24 (a GH62 arabinofuranosidase) releases at least 4 times more percentsolubilised xylose than the GH10 or GH11 xylanase alone.

Example 25: Hydrolysis of Defatted Destarched Maize (DFDSM) Using aCombination of a GH10 Xylanase and a GH62 Arabinofuranosidase

Defatted destarched maize (DFDSM, 400 mg) was added to aqueous sodiumacetate (0.1 M, 3.9 mL) solution containing calcium chloride (5 mM) atpH 5 and the mixture heated to 40° C. for 30 minutes. 1004 buffer orenzyme solution was added and the sample was heated at 40° C. for 4hours. The sample was cooled to 5° C. and centrifuged (4000 rpm, 5° C.)for 10 minutes. 1.7 mL of the sample was transferred to an Eppendorftube and the enzyme deactivated by heating to 95° C. for 10 minutes. Thesamples were then frozen until hydrolysed (within 72 hours and xylosedetermination was performed immediately after hydrolysis).

The supernatant was thawed and centrifuged (14000 rpm) for 5 minutes.The supernatant (250 μL) was diluted with Milli-Q water (250 μL) inglass tubes and HCl (1.63 M, 2.0 mL) was added. The reaction was heatedto 100° C. for 1 hour then cooled in an ice bath. Aqueous NaOH solution(1.3 M, 2.5 mL) was added whilst the samples were cooled on ice and thesamples were stored at 0-5° C. whilst xylose content was analysed usingthe xylose assay. The results are presented in tables 5, 6, 7, 8 and 9.

TABLE 5 Xylose release from DFDSM using a GH10 xylanase (SEQ ID NO: 72)and two different GH62 arabinofuranosidases (SEQ ID NO: 24 or 63) Conc.Conc. Percent [mg [mg Soluble solubilised GH10 Xylanase EP/kg] GH62Arabinofuranosidase EP/kg] xylose (%) xylose¹ SEQ ID NO: 72 10 None —0.26 1.9 SEQ ID NO: 72 10 None — 0.26 1.9 SEQ ID NO: 72 10 None — 0.201.4 SEQ ID NO: 72 10 SEQ ID NO: 24 10 0.90 6.1 SEQ ID NO: 72 10 SEQ IDNO: 63 10 0.84 5.9 Table 5 shows the amount of xylose measured afteracid hydrolysis of supernatants (% of dry matter and % solubilizedxylose of total xylose) when incubating DFDSM with SEQ ID NO: 72 (a GH10xylanase) alone or in combination with a GH62 arabinofuranosidase (SEQID NO: 24 or 63). ¹Percentage solubilised xylose was calculated asdescribed in example 23.

TABLE 6 Xylose release from DFDSM using a GH10 xylanase (SEQ ID NO: 72)and a GH62 arabinofuranosidase (SEQ ID NO: 24) Conc. Conc. Percent [mg[mg Soluble solubilised GH10 Xylanase EP/kg] GH62 ArabinofuranosidaseEP/kg] xylose (%) xylose¹ SEQ ID NO: 72 10 None — 0.29 1.9 SEQ ID NO: 7210 SEQ ID NO: 24 10 1.22 8.2 SEQ ID NO: 72 10 SEQ ID NO: 24 10 1.20 8.0Table 6 shows the amount of xylose measured after acid hydrolysis ofsupernatants (% of dry matter and % solubilized xylose of total xylose)when incubating DFDSM with SEQ ID NO: 72 (a GH10 xylanase) alone or incombination with a GH62 arabinofuranosidase (SEQ ID NO: 24). ¹Percentagesolubilised xylose was calculated as described in example 23.

TABLE 7 Xylose release from DFDSM using a GH10 xylanase (SEQ ID NO: 72)and a GH62 arabinofuranosidase (SEQ ID NO: 24) Conc. Conc. Percent [mg[mg Soluble solubilised GH10 Xylanase EP/kg] GH62 ArabinofuranosidaseEP/kg] xylose (%) xylose¹ SEQ ID NO: 72 10 None — 0.30 2.0 SEQ ID NO: 7210 SEQ ID NO: 24 10 1.20 8.1 Table 7 shows the amount of xylose measuredafter acid hydrolysis of supernatants (% of dry matter and % solubilizedxylose of total xylose) when incubating DFDSM with SEQ ID NO: 72 (a GH10xylanase) alone or in combination with a GH62 arabinofuranosidase (SEQID NO: 24). ¹Percentage solubilised xylose was calculated as describedin example 23.

TABLE 8 Xylose release from DFDSM using a GH10 xylanase (SEQ ID NO: 70or 72) and a GH62 arabinofuranosidases (SEQ ID NO: 9) Conc. Conc.Percent [mg [mg Soluble solubilised GH10 Xylanase EP/kg] GH62Arabinofuranosidase EP/kg] xylose (%) xylose¹ SEQ ID NO: 70 25 None —0.16 1.1 SEQ ID NO: 72 25 None — 0.42 2.8 None — SEQ ID NO: 9 12.5 0.020.2 SEQ ID NO: 70 25 SEQ ID NO: 9 12.5 0.60 3.3 SEQ ID NO: 72 25 SEQ IDNO: 9 12.5 1.32 9.1 Table 8 shows the amount of xylose measured afteracid hydrolysis of supernatants (% of dry matter and % solubilizedxylose of total xylose) when incubating DFDSM with SEQ ID NO: 70 or 72(a GH10 xylanase) alone or in combination with a GH62arabinofuranosidase (SEQ ID NO: 9). ¹Percentage solubilised xylose wascalculated as described in example 23.

TABLE 9 Xylose release from DFDSM using a GH10 xylanase (SEQ ID NO: 71)and a GH62 arabinofuranosidases (SEQ ID NO: 21) Conc. Conc. Percent [mgGH62 [mg Soluble solubi- GH10 EP/ Arabino- EP/ xylose lised Xylanase kg]furanosidase kg] (%) xylose¹ SEQ ID NO: 71 10 None — 0.54 3.5 SEQ ID NO:71 10 None — 0.54 3.4 SEQ ID NO: 71 10 SEQ ID NO: 21 10 1.28 8.4 Table 9shows the amount of xylose measured after acid hydrolysis ofsupernatants (% of dry matter and % solubilized xylose of total xylose)when incubating DFDSM with SEQ ID NO: 71 (a GH10 xylanase) alone or incombination with a GH62 arabinofuranosidase (SEQ ID NO: 21). ¹Percentagesolubilised xylose was calculated as described in example 23.Conclusion

The results show that the percent solubilised xylose is significantlyhigher (at least 2 times) for all of the combinations of GH10 xylanaseand GH62 arabinofuranosidase tested compared to the GH10 xylanase alone.

Example 26: Hydrolysis of Defatted Destarched Maize (DFDSM) Using aCombination of a GH11 Xylanase and a GH62 Arabinofuranosidase

Defatted destarched maize (DFDSM, 400 mg) was added to aqueous sodiumacetate (0.1 M, 3.9 mL) solution containing calcium chloride (5 mM) atpH 5 and the mixture heated to 40° C. for 30 minutes. 1004 buffer orenzyme solution was added and the sample was heated at 40° C. for 4hours. The sample was cooled to 5° C. and centrifuged (4000 rpm, 5° C.)for 10 minutes. 1.7 mL of the sample was transferred to an Eppendorftube and the enzyme deactivated by heating to 95° C. for 10 minutes. Thesamples were then frozen until hydrolysed (within 72 hours and xylosedetermination was performed immediately after hydrolysis).

The supernatant was thawed and centrifuged (14000 rpm) for 5 minutes.The supernatant (2504) was diluted with Milli-Q water (250 μL) in glasstubes and HCl (1.63 M, 2.0 mL) was added. The reaction was heated to100° C. for 1 hour then cooled in an ice bath. Aqueous NaOH solution(1.3 M, 2.5 mL) was added whilst the samples were cooled on ice and thesamples were stored at 0-5° C. whilst xylose content was analysed usingthe xylose assay. The results are presented in tables 10 to 18inclusive.

TABLE 10 Xylose release from DFDSM using a GH11 xylanase (SEQ ID NO: 73)and two different GH62 arabinofuranosidases (SEQ ID NO: 9 or 12) Conc.Conc. Percent [mg GH62 [mg Soluble solubi- GH11 EP/ Arabino- EP/ xyloselised Xylanase kg] furanosidase kg] (%) xylose¹ SEQ ID NO: 73 25 None —0.09 0.5 None — SEQ ID NO: 12 12.5 0.02 0.1 None — SEQ ID NO: 9 12.50.04 0.1 SEQ ID NO: 73 25 SEQ ID NO: 12 12.5 0.58 3.8 SEQ ID NO: 73 25SEQ ID NO: 9 12.5 0.52 3.4 Table 10 shows the amount of xylose measuredafter acid hydrolysis of supernatants (% of dry matter and % solubilizedxylose of total xylose) when incubating DFDSM with SEQ ID NO: 73 (a GH11xylanase) alone or in combination with a GH62 arabinofuranosidase (SEQID NO: 9 or 12). ¹Percentage solubilised xylose was calculated asdescribed in example 23.

TABLE 11 Xylose release from DFDSM using a GH11 xylanase (SEQ ID NO: 73)and four different GH62 arabinofuranosidases (SEQ ID NO: 9, 15, 18 or21) Conc. Conc. Percent [mg GH62 [mg Soluble solubi- GH11 EP/ Arabino-EP/ xylose lised Xylanase kg] furanosidase kg] (%) xylose¹ SEQ ID NO: 7325 None — 0.08 0.1 SEQ ID NO: 73 25 SEQ ID NO: 15 12.5 0.43 2.9 SEQ IDNO: 73 25 SEQ ID NO: 18 12.5 0.48 3.3 SEQ ID NO: 73 25 SEQ ID NO: 2112.5 0.58 4.0 SEQ ID NO: 73 25 SEQ ID NO: 9 12.5 0.56 3.9 Table 11 showsthe amount of xylose measured after acid hydrolysis of supernatants (%of dry matter and % solubilized xylose of total xylose) when incubatingDFDSM with SEQ ID NO: 73 (a GH11 xylanase) alone or in combination witha GH62 arabinofuranosidase (SEQ ID NO: 9, 15, 18 or 21). ¹Percentagesolubilised xylose was calculated as described in example 23.

TABLE 12 Xylose release from DFDSM using a GH11 xylanase (SEQ ID NO: 73,75, 81 or 84) and two different GH62 arabinofuranosidases (SEQ ID NO: 9or 12) Conc. Conc. Percent [mg GH62 [mg Soluble solubi- GH11 EP/Arabino- EP/ xylose lised Xylanase kg] furanosidase kg] (%) xylose¹ SEQID NO: 73 25 None — 0.07 0.3 SEQ ID NO: 73 25 None — 0.09 0.5 SEQ ID NO:75 25 None — 0.21 1.3 SEQ ID NO: 75 25 None — 0.16 0.9 SEQ ID NO: 81 25None — 0.32 2.1 SEQ ID NO: 81 25 None — 0.39 2.6 SEQ ID NO: 87 25 None —0.31 2.0 SEQ ID NO: 87 25 None — 0.25 1.7 None — SEQ ID NO: 9 12.5 0.070.3 None — SEQ ID NO: 9 12.5 0.04 0.1 None — SEQ ID NO: 9 12.5 0.02 0.1None — SEQ ID NO: 9 12.5 0.03 0.1 None — SEQ ID NO: 12 12.5 0.02 0.0None — SEQ ID NO: 12 12.5 0.03 0.1 None — SEQ ID NO: 12 12.5 0.02 0.1None — SEQ ID NO: 12 12.5 0.02 0.0 SEQ ID NO: 73 25 SEQ ID NO: 9 12.50.53 3.5 SEQ ID NO: 73 25 SEQ ID NO: 12 12.5 0.48 3.1 SEQ ID NO: 75 25SEQ ID NO: 9 12.5 0.80 5.3 SEQ ID NO: 75 25 SEQ ID NO: 12 12.5 0.78 5.1SEQ ID NO: 81 25 SEQ ID NO: 9 12.5 0.97 6.5 SEQ ID NO: 81 25 SEQ ID NO:12 12.5 1.00 6.7 SEQ ID NO: 87 25 SEQ ID NO: 9 12.5 0.89 5.9 SEQ ID NO:87 25 SEQ ID NO: 12 12.5 0.87 5.8 Table 12 shows the amount of xylosemeasured after acid hydrolysis of supernatants (% of dry matter and %solubilized xylose of total xylose) when incubating DFDSM with SEQ IDNO: 73, 75, 81 or 84 (a GH11 xylanase) alone or in combination with aGH62 arabinofuranosidase (SEQ ID NO: 9 or 12). ¹Percentage solubilisedxylose was calculated as described in example 23.

TABLE 13 Xylose release from DFDSM using a GH11 xylanase (SEQ ID NO: 74)and a GH62 arabinofuranosidases (SEQ ID NO: 9) Conc. Conc. Percent [mgGH62 [mg Soluble solubi- GH11 EP/ Arabino- EP/ xylose lised Xylanase kg]furanosidase kg] (%) xylose¹ SEQ ID NO: 74 25 None — 0.17 1.2 None — SEQID NO: 9 12.5 0.02 0.2 SEQ ID NO: 74 25 SEQ ID NO: 9 12.5 0.75 5.1 Table13 shows the amount of xylose measured after acid hydrolysis ofsupernatants (% of dry matter and % solubilized xylose of total xylose)when incubating DFDSM with SEQ ID NO: 74 (a GH11 xylanase) alone or incombination with a GH62 arabinofuranosidase (SEQ ID NO: 9). ¹Percentagesolubilised xylose was calculated as described in example 23.

TABLE 14 Xylose release from DFDSM using a GH11 xylanase (SEQ ID NO: 78)and three different GH62 arabinofuranosidases (SEQ ID NO: 51, 57 or 69)Conc. Conc. Percent [mg GH62 [mg Soluble solubi- GH11 EP/ Arabino- EP/xylose lised Xylanase kg] furanosidase kg] (%) xylose¹ SEQ ID NO: 78 10None — 0.33 2.3 SEQ ID NO: 78 10 SEQ ID NO: 51 10 0.96 6.5 SEQ ID NO: 7810 SEQ ID NO: 57 10 1.13 7.6 SEQ ID NO: 78 10 SEQ ID NO: 69 10 1.17 7.9Table 14 shows the amount of xylose measured after acid hydrolysis ofsupernatants (% of dry matter and % solubilized xylose of total xylose)when incubating DFDSM with SEQ ID NO: 78 (a GH11 xylanase) alone or incombination with a GH62 arabinofuranosidase (SEQ ID NO: 51, 57 or 69).¹Percentage solubilised xylose was calculated as described in example23.

TABLE 15 Xylose release from DFDSM using a GH11 xylanase (SEQ ID NO: 78)and three different GH62 arabinofuranosidases (SEQ ID NO: 27. 45 or 63)Conc. Conc. Percent [mg GH62 [mg Soluble solubi- GH11 EP/ Arabino- EP/xylose lised Xylanase kg] furanosidase kg] (%) xylose¹ SEQ ID NO: 78 10None — 0.36 2.4 SEQ ID NO: 78 10 None — 0.31 2.0 SEQ ID NO: 78 10 SEQ IDNO: 27 10 1.31 8.1 SEQ ID NO: 78 10 SEQ ID NO: 45 10 0.94 6.2 SEQ ID NO:78 10 SEQ ID NO: 63 10 0.99 6.6 Table 15 shows the amount of xylosemeasured after acid hydrolysis of supernatants (% of dry matter and %solubilized xylose of total xylose) when incubating DFDSM with SEQ IDNO: 78 (a GH11 xylanase) alone or in combination with a GH62arabinofuranosidase (SEQ ID NO: 27, 45 or 63). ¹Percentage solubilisedxylose was calculated as described in example 23.

TABLE 16 Xylose release from DFDSM using a GH11 xylanase (SEQ ID NO: 73or 78) and a GH62 arabinofuranosidases (SEQ ID NO: 21) Conc. Conc.Percent [mg GH62 [mg Soluble solubi- GH11 EP/ Arabino- EP/ xylose lisedXylanase kg] furanosidase kg] (%) xylose¹ SEQ ID NO: 73 25 None — 0.100.5 SEQ ID NO: 78 10 None — 0.33 2.1 SEQ ID NO: 73 25 SEQ ID NO: 21 100.58 3.7 SEQ ID NO: 78 10 SEQ ID NO: 21 10 1.03 6.8 Table 16 shows theamount of xylose measured after acid hydrolysis of supernatants (% ofdry matter and % solubilized xylose of total xylose) when incubatingDFDSM with SEQ ID NO: 78 (a GH11 xylanase) alone or in combination witha GH62 arabinofuranosidase (SEQ ID NO: 27, 45 or 63). ¹Percentagesolubilised xylose was calculated as described in example 23.

TABLE 17 Xylose release from DFDSM using a GH11 xylanase (SEQ ID NO: 88)and four different GH62 arabinofuranosidases (SEQ ID NO: 9, 12, 24 or27) Conc. Conc. Percent [mg GH62 [mg Soluble solubi- GH11 EP/ Arabino-EP/ xylose lised Xylanase kg] furanosidase kg] (%) xylose¹ None — None —0 0 SEQ ID NO: 88 10 None — 0.09 0.5 SEQ ID NO: 88 10 SEQ ID NO: 27 100.65 4.4 SEQ ID NO: 88 10 SEQ ID NO: 24 10 1.22 8.2 SEQ ID NO: 88 10 SEQID NO: 9 10 0.57 3.8 SEQ ID NO: 88 10 SEQ ID NO: 12 10 0.50 3.3 Table 17shows the amount of xylose measured after acid hydrolysis ofsupernatants (% of dry matter and % solubilized xylose of total xylose)when incubating DFDSM with SEQ ID NO: 88 (a GH11 xylanase) alone or incombination with a GH62 arabinofuranosidase (SEQ ID NO: 9, 12, 24 or27). ¹Percentage solubilised xylose was calculated as described inexample 23.

TABLE 18 Xylose release from DFDSM using a GH11 xylanase (SEQ ID NO: 89)and four different GH62 arabinofuranosidases (SEQ ID NO: 9, 12, 24 or27) Conc. Conc. Percent [mg GH62 [mg Soluble solubi- GH11 EP/ Arabino-EP/ xylose lised Xylanase kg] furanosidase kg] (%) xylose¹ None — None —0 0 SEQ ID NO: 89 10 None — 0.07 0.5 SEQ ID NO: 89 10 SEQ ID NO: 27 100.36 2.4 SEQ ID NO: 89 10 SEQ ID NO: 24 10 0.76 5.1 SEQ ID NO: 89 10 SEQID NO: 9 10 0.43 2.9 SEQ ID NO: 89 10 SEQ ID NO: 12 10 0.35 2.3 Table 18shows the amount of xylose measured after acid hydrolysis ofsupernatants (% of dry matter and % solubilized xylose of total xylose)when incubating DFDSM with SEQ ID NO: 89 (a GH11 xylanase) alone or incombination with a GH62 arabinofuranosidase (SEQ ID NO: 9, 12, 24 or27). ¹Percentage solubilised xylose was calculated as described inexample 23.Conclusion

The results show that the percent solubilised xylose is significantlyhigher (at least 2 times) for all of the combinations of GH11 xylanaseand GH62 arabinofuranosidase tested compared to the GH11 xylanase alone.

Example 27: Hydrolysis of Defatted Destarched Maize (DFDSM) Using aCombination of a Commercial Animal Feed Xylanase and a GH62Arabinofuranosidase

Defatted destarched maize (DFDSM, 400 mg) was added to aqueous sodiumacetate (0.1 M, 3.9 mL) solution containing calcium chloride (5 mM) atpH 5 and the mixture heated to 40° C. for 30 minutes. 10 μL buffer orenzyme solution was added and the sample was heated at 40° C. for 4hours. The sample was cooled to 5° C. and centrifuged (4000 rpm, 5° C.)for 10 minutes. 1.7 mL of the sample was transferred to an Eppendorftube and the enzyme deactivated by heating to 95° C. for 10 minutes. Thesamples were then frozen until hydrolysed (within 72 hours and xylosedetermination was performed immediately after hydrolysis).

The supernatant was thawed and centrifuged (14000 rpm) for 5 minutes.The supernatant (250 μL) was diluted with Milli-Q water (250 μL) inglass tubes and HCl (1.63 M, 2.0 mL) was added. The reaction was heatedto 100° C. for 1 hour then cooled in an ice bath. Aqueous NaOH solution(1.3 M, 2.5 mL) was added whilst the samples were cooled on ice and thesamples were stored at 0-5° C. whilst xylose content was analysed usingthe xylose assay. The results are presented in tables 19, 20 and 21

TABLE 19 Xylose release from DFDSM using Rovabio Excel and fourdifferent GH62 arabinofuranosidases (SEQ ID NO: 9, 12, 24 or 27) Conc.Percent [mg Soluble solubi- Conc. Arabino- EP/ xylose lised Xylanase[ppm] furanosidase kg] (%) xylose¹ Rovabio 50 ppm None — 0.01 0.1 ExcelAP Rovabio 50 ppm SEQ ID NO: 27 10 0.07 0.5 Excel AP Rovabio 50 ppm SEQID NO: 24 10 0.13 0.9 Excel AP Rovabio 50 ppm SEQ ID NO: 9 10 0.08 0.5Excel AP Rovabio 50 ppm SEQ ID NO: 12 10 0.06 0.4 Excel AP Table 19shows the amount of xylose measured after acid hydrolysis ofsupernatants (% of dry matter and % solubilized xylose of total xylose)when incubating DFDSM with Rovabio Excel AP alone or in combination witha GH62 arabinofuranosidase (SEQ ID NO: 9, 12, 24 or 27). Rovabio ExcelAP is available from Adisseo and the product declaration states that ithas xylanase activity and endo-1,3(4)-beta-glucanase activity.¹Percentage solubilised xylose was calculated as described in example23.

TABLE 20 Xylose release from DFDSM using Econase XT and four differentGH62 arabinofuranosidases (SEQ ID NO: 9, 12, 24 or 27) Conc. Percent [mgSoluble solubi- Conc. Arabino- EP/ xylose lised Xylanase [ppm]furanosidase kg] (%) xylose¹ Econase 150 ppm None — 0.04 0.1 XT 25Econase 150 ppm SEQ ID NO: 27 10 0.20 1.2 XT 25 Econase 150 ppm SEQ IDNO: 24 10 0.46 3.0 XT 25 Econase 150 ppm SEQ ID NO: 9 10 0.18 1.1 XT 25Econase 150 ppm SEQ ID NO: 12 10 0.14 0.8 XT 25 Table 20 shows theamount of xylose measured after acid hydrolysis of supernatants (% ofdry matter and % solubilized xylose of total xylose) when incubatingDFDSM with Econase XT 25 alone or in combination with a GH62arabinofuranosidase (SEQ ID NO: 9, 12, 24 or 27). Econase XT 25 isavailable from AB Enzymes and the product declaration states that it hasendo-1,4-beta-xylanase activity. ¹Percentage solubilised xylose wascalculated as described in example 23.

TABLE 21 Xylose release from DFDSM using Belfeed and four different GH62arabinofuranosidases (SEQ ID NO: 9, 12, 24 or 27) Conc. Percent [mgSoluble solubi- Conc. Arabino- EP/ xylose lised Xylanase [ppm]furanosidase kg] (%) xylose¹ Belfeed B 100 ppm None — 0.04 0.2 1100 MPBelfeed B 100 ppm SEQ ID NO: 27 10 0.21 1.3 1100 MP Belfeed B 100 ppmSEQ ID NO: 24 10 0.38 2.5 1100 MP Belfeed B 100 ppm SEQ ID NO: 9 10 0.211.3 1100 MP Belfeed B 100 ppm SEQ ID NO: 12 10 0.18 1.1 1100 MP Table 21shows the amount of xylose measured after acid hydrolysis ofsupernatants (% of dry matter and % solubilized xylose of total xylose)when incubating DFDSM with Belfeed B 1100 MP alone or in combinationwith a GH62 arabinofuranosidase (SEQ ID NO: 9, 12, 24 or 27). Belfeed B1100 MP is available from Beldem and the product declaration states thatit has specific pentosanase endo-1,4-beta-xylanase (EC 3.2.1.8)activity. ¹Percentage solubilised xylose was calculated as described inexample 23.Conclusion

The results show that the percent solubilised xylose is significantlyhigher (at least 2 times) for all of the combinations of thecommercially available xylanases and GH62 arabinofuranosidase testedcompared to the commercially available xylanase alone.

Example 28: Cloning of GH11 Xylanase from Lasiodiplodia theobromae (SEQID NO: 99)

The xylanase with nucleotide sequence SEQ ID NO: 97 was PCR amplifiedfrom genomic DNA isolated from Lasiodiplodia theobromae and cloned intothe expression vector pSUN515, which is a derivative of pCaHj505(WO2013029496).

The final expression plasmid was transformed into the Aspergillus oryzaeMT3568 expression host. A. oryzae MT3568 is a derivative of A. oryzaeJaL355 (WO02/40694) in which pyrG auxotrophy was restored by disruptingthe A. oryzae acetamidase (amdS) gene with the pyrG gene. The xylanasegene was integrated by homologous recombination into the A. oryzaeMT3568 host cell genome upon transformation.

The gene coding for amdS was used as marker. Transformants were selectedon pyrG media agar supplemented with 10 mM acetamide. One recombinantAspergillus oryzae clone containing the xylanase expression constructwas selected and was cultivated on a rotary shaking table in 4 2-literbaffled Erlenmeyer flasks each containing 400 ml YPM (1% Yeast extract,2% Peptone and 2% Maltose). After 3 days cultivation time at 30° C.,enzyme containing supernatants were harvested by filtration using a 0.22μm 1-liter bottle top vacuum filter (Corning Inc., Corning, N.Y., USA).

Example 29: Purification of GH11 Xylanase from Lasiodiplodia theobromae(SEQ ID NO: 99)

A 1600 ml volume of filtered supernatant of Aspergillus oryzae (example32) was precipitated with ammonium sulfate (80% saturation),re-dissolved in 50 ml of 20 mM Tris-HCl pH 7.5, dialyzed against thesame buffer, and filtered through a 0.45 μm filter. The final volume was75 ml. The solution was applied to a 40 ml Q SEPHAROSE® Fast Flow column(GE Healthcare, Buckinghamshire, UK) equilibrated with 20 mM Tris-HCl pH7.5. Proteins were eluted with a linear 0-0.25 M NaCl gradient.Fractions were analyzed by SDS-PAGE using a NUPAGE® NOVEX® 4-12%Bis-Tris Gel with 50 mM MES. The resulting gel was stained withINSTANTBLUE™. Fractions containing a band at approximately 22 kDa werepooled. Then the pooled solution was concentrated by ultrafiltration.

Example 30: Cloning of a GH10 Xylanase from Ascobolus stictoideus (SEQID NO: 102)

The xylanase with nucleotide sequence SEQ ID NO: 100 and the peptidetranslation of the protein shown in SEQ ID NO: 101 was PCR amplifiedfrom genomic DNA isolated from Ascobolus stictoideus and cloned into theexpression vector pDAu222 as described in WO 2013024021 using BamHI andXhoI restriction sites.

The sequence of the xylanase encoding gene cloned in the expressionvector was confirmed and the expression construct was transformed intothe Aspergillus oryzae strain MT3568 (WO 11/057140) to produce thesecreted mature peptide with protein sequence SEQ ID NO: 102.Transformants were selected on acetamide during regeneration fromprotoplasts and subsequently re-isolated under selection (Christensen etal., 1988, Biotechnology 6, 1419-1422 and WO 04/032648).

For production of the recombinant xylanase, a single Aspergillustransformant was cultured in six 500 ml baffled flasks each containing180 ml of DAP-4C-1 medium (WO 12/103350). The cultures were shaken on arotary table at 150 RPM at 26° C. for 3 days. The culture brothsubsequently was separated from cellular material by passage through a0.22 um filter.

Example 31: Purification of the GH10 Xylanase from Ascobolus stictoideus(SEQ ID NO: 102)

The filtered broth was buffer exchanged with HEPES (50 mM, pH 7) using aQuixStand Tangential flow ultrafiltration system fitted with a 10 KDacut-off cartridge (GE Healthcare, QuixStand Product code: QSM-02SP/50;10 KDa Cartridge Product code: UFP-10E-4MA). The buffer exchanged samplewas loaded onto a column packed with UNOsphereTMQ (Bio-Rad Laboratories,Hercules, Calif.; Catalogue No: 156-0105) which was equilibrated withthe same buffer as that used for the buffer exchange of the sample.After wash with equilibration buffer, bound protein was eluted withstep-wise increase of NaCl concentration in following order: 50 mM, 100mM, 200 mM, 500 mM and 1000 mM. All the fractions including flow throughand wash were collected and analyzed by SDS-PAGE. On analysis, it wasobserved that the purified sample was in the flow through. The flowthrough was concentrated using the same Ultrafiltration system asmention above. The quantity of the purified sample was determinedspectrometrically (A280) and analyzed using SDS-PAGE.

Example 32: Cloning of GH62 Arabinofuranosidases from Penicilliumsoppii, Aspergillus aculeatus, Aspergillus fumigatiaffinis, Neosartoryafischeri, Thielavia arenaria, Thielavia terricola, Chaetomiumolivicolor, Curvularia geniculata, Drechslera sp., and Humicola sp. (SEQID NO: 105, 123, 138, 147, 156, 159, 162, 165, 168, 171 and 174)

The arabinofuranosidase encoding genes with the nucleotide sequences SEQID NO: 145, 136, 154, 157, 160, 169, 166, 163, 121, 103 and 172 were PCRamplified from genomic DNA isolated from Penicillium soppii, Aspergillusaculeatus, Aspergillus fumigatiaffinis, Neosartorya fischeri, Thielaviaarenaria, Thielavia terricola, Chaetomium olivicolor, Curvulariageniculata, Drechslera sp., and Humicola sp. and cloned into theAspergillus expression vector pMStr57 (WO 04/032648).

The sequences of the arabinofuranosidase encoding genes cloned in theexpression vector were confirmed, and the expression constructs weretransformed into the Aspergillus oryzae strain MT3568 (WO 11/057140).Transformants were selected on acetamide during regeneration fromprotoplasts and subsequently re-isolated under selection (Christensen etal., 1988, Biotechnology 6, 1419-1422 and WO 04/032648).

For production of the recombinant arabinofuranosidases, a singleAspergillus transformant was selected for each arabinofuranosidase andthe transformants were cultured in 500 ml baffled flasks containing 150ml of DAP-4C-1 medium (WO 12/103350). The cultures were shaken on arotary table at 150 RPM at 30° C. for 4 days. The culture broth wassubsequently separated from cellular material by passage through a 0.22um filter.

Example 33: Purification of GH62 Arabinofuranosidases from PenicilliumAspergillus aculeatus, Aspergillus fumigatiaffinis, Neosartoryafischeri, Thielavia arenaria, Thielavia terricola, Chaetomiumolivicolor, Curvularia geniculata, Drechslera sp., and Humicola sp. (SEQID NO: 105, 123, 138, 147, 156, 159, 162, 165, 168, 171 and 174)

The filtrated sample was adjusted to around pH 7.5 and 1.8M ammoniumsulfate was added. The sample was applied to a 5 ml HiTrap™ Phenyl (HS)column on an Akta Explorer. Prior to loading, the column had beenequilibrated in 5 column volumes (CV) of 50 mM HEPES+1.8M AMS pH 7. Inorder to remove unbound material, the column was washed with 5 CV of 50mM HEPES+1.8M AMS pH 7. The target protein was eluted from the columninto a 10 ml loop using 50 mM HEPES+20% isopropanol pH 7. From the loop,the sample was loaded onto a desalting column (HiPrep™ 26/10 Desalting),which had been equilibrated with 3 CV of 50 mM HEPES+100 mM NaCl pH 7.0.The target protein was eluted with 50 mM HEPES+100 mM NaCl pH 7.0 andrelevant fractions were selected and pooled based on the chromatogram.The flow rate was 5 ml/min.

Example 34: Cloning of GH62 Arabinofuranosidases from Xylanibacteriumsp-61981 and Glycomyces rutgersensis (SEQ ID NO: 111 and 129)

The bacterial GH62 sequences from Xylanibacterium sp-61981 (SEQ ID NO:106) and Glycomyces rutgersensis (SEQ ID NO: 124) were cloned into aBacillus expression vector as described in example 8 to give the His-tagsequence operably linked to the mature wild type AraF sequence andBacillus clausii secretion signal as shown in SEQ ID NO: 109 and SEQ IDNO: 127 respectively. The gene construct was then expressed as describedin example 8.

Example 35: Purification of GH62 Arabinofuranosidases fromXylanibacterium sp-61981 and Glycomyces rutgersensis (SEQ ID NO: 111 and129)

pH was adjusted to pH 8, filtrated through a 0.2 μM, and the supernatantapplied to a 5 ml HisTrap™ excel column. Prior to loading, the columnhad been equilibrated in 5 column volumes (CV) of 50 mM Tris/HCl pH 8.In order to remove unbound material, the column was washed with 8 CV of50 mM Tris/HCl pH 8, and elution of the target was obtained with 50 mMHEPES pH 7+10 mM imidazole. The eluted protein was desalted on a HiPrep™26/10 desalting column, equilibrated using 3 CV of 50 mM HEPES pH 7+100mM NaCl. This buffer was also used for elution of the target, and theflow rate was 10 ml/min. Relevant fractions were selected and pooledbased on the chromatogram and SDS-PAGE analysis.

Example 36: Cloning of a GH62 Arabinofuranosidase from Microdochiumnivale (SEQ ID NO: 117)

An arabinofuranosidase encoding gene with the nucleotide sequence SEQ IDNO: 112 was PCR amplified from genomic DNA isolated from Microdochiumnivale and cloned into the Aspergillus expression vector pMStr366. Thevector pMStr366 is a version of the expression vector pMStr57 (WO04/032648) that has been modified to allow fusion of an insert CDS to avector-encoded HIS tag with the sequence RHHHHHHP (SEQ ID NO: 91). Thenucleotide sequence of the resulting fusion is shown in SEQ ID NO: 115and the peptide translation of the His-tagged protein is shown in SEQ IDNO: 116.

The sequence of the tagged arabinofuranosidase encoding gene cloned inthe expression vector was confirmed, and the expression construct wastransformed into the Aspergillus oryzae strain MT3568 (WO 11/057140).Transformants were selected on acetamide during regeneration fromprotoplasts and subsequently re-isolated under selection (Christensen etal., 1988, Biotechnology 6, 1419-1422 and WO 04/032648).

For production of the recombinant arabinofuranosidase, a singleAspergillus transformant was selected, and the transformant was culturedin 500 ml baffled flasks containing 100 ml of YPG medium (WO 05/066338).The cultures were shaken on a rotary table at 150 RPM at 30° C. for 4days. The culture broth was subsequently separated from cellularmaterial by passage through a 0.22 um filter.

Example 37: Cloning of a GH62 Arabinofuranosidase from Microdochiumnivale (SEQ ID NO: 117)

The GH62 arabinofuranosidases were purified as described in example 35.

Example 38: Cloning of a GH62 Arabinofuranosidase from Humicolahyalothermophila (SEQ ID NO: 120)

The arabinofuranosidase with nucleotide sequence SEQ ID NO: 118 was PCRamplified from genomic DNA isolated from Humicola hyalothermophila andcloned into the expression vector pSUN515, which is a derivative ofpCaHj505 (WO2013029496).

The final expression plasmid was transformed into the Aspergillus oryzaeMT3568 expression host. A. oryzae MT3568 is a derivative of A. oryzaeJaL355 (WO02/40694) in which pyrG auxotrophy was restored by disruptingthe A. oryzae acetamidase (amdS) gene with the pyrG gene. Thearabinofuranosidase gene was integrated by homologous recombination intothe A. oryzae MT3568 host cell genome upon transformation.

The gene coding for amdS was used as marker. Transformants were selectedon pyrG media agar supplemented with 10 mM acetamide. One recombinantAspergillus oryzae clone containing the arabinofuranosidase expressionconstruct was selected and was cultivated on a rotary shaking table in 42-liter baffled Erlenmeyer flasks each containing 400 ml YPM (1% Yeastextract, 2% Peptone and 2% Maltose). After 3 days cultivation time at30° C., enzyme containing supernatants were harvested by filtrationusing a 0.22 μm 1-liter bottle top vacuum filter (Corning Inc., Corning,N.Y., USA).

Example 39: Purification of the GH62 Arabinofuranosidase from Humicolahyalothermophila (SEQ ID NO: 120)

A 1400 ml volume of filtered supernatant was precipitated with ammoniumsulfate (80% saturation), re-dissolved in 50 ml of 20 mM Bis-Tris pH6.0, dialyzed against the same buffer, and filtered through a 0.45 μmfilter. The final volume was 80 ml. The solution was applied to a 50 mlQ SEPHAROSE® Fast Flow column (GE Healthcare, Buckinghamshire, UK)equilibrated with 20 mM Bis-Tris pH 6.0. Proteins were eluted with alinear 0-0.25 M NaCl gradient. Fractions were analyzed by SDS-PAGE usinga Mini-PROTEAN TGX Stain-Free 4-15% Precast Gel (Bio-Rad Laboratories,CA, United States). Fractions containing a band at approximately 39 kDawere pooled. Then the pooled solution was concentrated byultrafiltration.

Example 40: Cloning of GH62 Arabinofuranosidases from Coprinopsiscinerea, Remersonia thermophile and Bipolaris sorokiniana (SEQ ID NO:135, 144 and 153)

The arabinofuranosidase encoding genes with the nucleotide sequences SEQID NO: 130, 139 and 148 were PCR amplified from genomic DNA isolatedfrom Coprinopsis cinerea, Remersonia thermophile and Bipolarissorokiniana and cloned into the Aspergillus expression vector pMStr366.The vector pMStr366 is a version of the expression vector pMStr57 (WO04/032648) that has been modified to allow fusion of an insert CDS to avector-encoded HIS tag with the sequence RHHHHHHP (SEQ ID NO: 91). Thenucleotide sequences of the resulting fusions are shown in SEQ ID NO:133, 142 and 151 and the peptide translations of the His-tagged proteinsare shown in SEQ ID NO: 134, 143 and 152.

The sequences of the tagged arabinofuranosidase encoding genes cloned inthe expression vector were confirmed, and the expression constructs weretransformed into the Aspergillus oryzae strain MT3568 (WO 11/057140).Transformants were selected on acetamide during regeneration fromprotoplasts and subsequently re-isolated under selection (Christensen etal., 1988, Biotechnology 6, 1419-1422 and WO 04/032648).

For production of the recombinant arabinofuranosidases, a singleAspergillus transformant was selected for each arabinofuranosidase andthe transformants were cultured in 500 ml baffled flasks containing 150ml of DAP-4C-1 medium (WO 12/103350). The cultures were shaken on arotary table at 150 RPM at 30° C. for 4 days. The culture broth wassubsequently separated from cellular material by passage through a 0.22um filter.

Example 41: Purification of the GH62 Arabinofuranosidases fromCoprinopsis cinerea and Remersonia thermophila (SEQ ID NO: 135 and 144)

The GH62 arabinofuranosidases were purified as described in example 35.

Example 42: Purification of the GH62 Arabinofuranosidase from Bipolarissorokiniana (SEQ ID NO: 153)

Filtrated broth was adjusted to pH7.0 and filtrated on 0.22 μm PESfilter (Nalge Nunc International, Nalgene labware cat #595-4520). Thefiltrate was loaded onto a MEP Hypercel™ column (Pall Corporation, LongIsland, N.Y., USA) equilibrated with 50 mM TRIS pH7.0. After wash withequilibration buffer, the bound proteins were batch eluted with 100 mMacetic acid pH 4.0. Fractions were collected and analyzed by SDS-PAGE.The fractions were pooled and applied to a Sephadex™ G-25 (medium) (GEHealthcare, Piscataway, N.J., USA) column equilibrated in 50 mM TRIS pH7.0. The fractions were then applied to a SOURCE™ 15S (GE Healthcare,Piscataway, N.J., USA) column equilibrated in 50 mM TRIS pH 7.0 andbound proteins were eluted with a linear gradient from 0-1000 mM sodiumchloride over 10 CV. Fractions were collected and analyzed by SDS-PAGE.

Example 43: Cloning of a GH10 Xylanase from Ustilago maydis (SEQ ID NO:180)

A xylanase encoding gene with the nucleotide sequence SEQ ID NO: 175 wasPCR amplified from genomic DNA isolated from Ustilago maydis and clonedinto the Aspergillus expression vector pMStr366. The vector pMStr366 isa version of the expression vector pMStr57 (WO 04/032648) that has beenmodified to allow fusion of an insert CDS to a vector-encoded HIS tagwith the sequence RHHHHHHP (SEQ ID NO: 91). The nucleotide sequence ofthe resulting fusion is shown in SEQ ID NO: 178 and the peptidetranslation of the His-tagged protein is shown in SEQ ID NO: 179.

The sequence of the tagged xylanase encoding gene cloned in theexpression vector was confirmed, and the expression construct wastransformed into the Aspergillus oryzae strain MT3568 (WO 11/057140).Transformants were selected on acetamide during regeneration fromprotoplasts and subsequently re-isolated under selection (Christensen etal., 1988, Biotechnology 6, 1419-1422 and WO 04/032648).

For production of the recombinant xylanase, a single Aspergillustransformant was selected and the transformant was cultured in 500 mlbaffled flasks containing 150 ml of DAP-4C-1 medium (WO 12/103350). Thecultures were shaken on a rotary table at 150 RPM at 30° C. for 3 days.The culture broth was subsequently separated from cellular material bypassage through a 0.45 um filter.

Example 44: Purification of the GH10 Xylanase from Ustilago maydis (SEQID NO: 180)

pH was adjusted to pH 8, filtrated through a 0.2 μM, and the supernatantapplied to a 5 ml HisTrap™ excel column. Prior to loading, the columnhad been equilibrated in 5 column volumes (CV) of 50 mM Tris/HCl pH 8.In order to remove unbound material, the column was washed with 8 CV of50 mM Tris/HCl pH 8, and elution of the target was obtained with 50 mMHEPES pH 7+10 mM imidazole. The eluted protein was desalted on a HiPrep™26/10 desalting column, equilibrated using 3 CV of 50 mM HEPES pH 7+100mM NaCl. This buffer was also used for elution of the target, and theflow rate was 10 ml/min. Relevant fractions were selected and pooledbased on the chromatogram and SDS-PAGE analysis.

Example 45: Hydrolysis of Defatted Destarched Maize (DFDSM) Using aCombination of a GH10 Xylanase and a GH62 Arabinofuranosidase

Defatted destarched maize (DFDSM, 400 mg) was added to aqueous sodiumacetate (0.1 M, 3.9 mL) solution containing calcium chloride (5 mM) atpH 5 and the mixture heated to 40° C. for 30 minutes. 1004 buffer orenzyme solution was added and the sample was heated at 40° C. for 4hours. The sample was cooled to 5° C. and centrifuged (4000 rpm, 5° C.)for 10 minutes. 1.7 mL of the sample was transferred to an Eppendorftube and the enzyme deactivated by heating to 95° C. for 10 minutes. Thesamples were then frozen until hydrolysed (within 72 hours and xylosedetermination was performed immediately after hydrolysis).

The supernatant was thawed and centrifuged (14000 rpm) for 5 minutes.The supernatant (250 μL) was diluted with Milli-Q water (250 μL) inglass tubes and HCl (1.63 M, 2.0 mL) was added. The reaction was heatedto 100° C. for 1 hour then cooled in an ice bath. Aqueous NaOH solution(1.3 M, 2.5 mL) was added whilst the samples were cooled on ice and thesamples were stored at 0-5° C. whilst xylose content was analysed usingthe xylose assay. The results are presented in table 22.

TABLE 22 Xylose release from DFDSM using a GH10 xylanase (SEQ ID NO: 95)and four different GH62 arabinofuranosidases (SEQ ID NO: 21, 24, 27 or44) Conc. Conc. Percent [mg GH62 [mg Soluble solubi- GH10 EP/ Arabino-EP/ xylose lised Xylanase kg] furanosidase kg] (%) xylose¹ Blank — None— 0.019 0.0 SEQ ID NO: 95 25 None — 0.164 1.0 SEQ ID NO: 95 25 SEQ IDNO: 24 12.5 0.385 2.5 SEQ ID NO: 95 25 SEQ ID NO: 44 12.5 0.374 2.4 SEQID NO: 95 25 SEQ ID NO: 27 12.5 0.325 2.1 SEQ ID NO: 95 25 SEQ ID NO: 2112.5 0.317 2.0 Table 22 shows the amount of xylose measured after acidhydrolysis of supernatants (% of dry matter and % solubilized xylose oftotal xylose) when incubating DFDSM with SEQ ID NO: 95 (a GH10 xylanasecorresponding to SEQ ID NO: 1 of WO2013/068550) alone or in combinationwith a GH62 arabinofuranosidase (SEQ ID NO: 21, 24, 27 or 44).¹Percentage solubilised xylose was calculated as described in example23.Conclusion

The results show that the percent solubilised xylose is significantlyhigher (at least 2 times) for all of the combinations of the prior artxylanase and GH62 arabinofuranosidase tested compared to the xylanasealone.

Example 46: Hydrolysis of Defatted Destarched Maize (DFDSM) Using aCombination of a GH11 Xylanase and a GH62 Arabinofuranosidase

The experiment was performed as described in example 45 and the resultsare presented in tables 23 to 27 inclusive.

TABLE 23 Xylose release from DFDSM using two different GH11 xylanases(SEQ ID NO: 73 or 74) and a GH62 arabinofuranosidase (SEQ ID NO: 24)Conc. Conc. Percent [mg GH62 [mg Soluble solubi- GH11 EP/ Arabino- EP/xylose lised Xylanase kg] furanosidase kg] (%) xylose¹ SEQ ID NO: 73 10None — 0.07² 0.3 SEQ ID NO: 74 10 None — 0.17 0.9 None — SEQ ID NO: 2410 0.09 0.3 SEQ ID NO: 73 10 SEQ ID NO: 24 10 0.93 6.0 SEQ ID NO: 73 10SEQ ID NO: 24 10 1.05 6.9 SEQ ID NO: 74 10 SEQ ID NO: 24 10 1.02 6.7Table 23 shows the amount of xylose measured after acid hydrolysis ofsupernatants (% of dry matter and % solubilized xylose of total xylose)when incubating DFDSM with SEQ ID NO: 73 or 74 (a GH11 xylanase) aloneor in combination with a GH62 arabinofuranosidase (SEQ ID NO: 24).¹Percentage solubilised xylose was calculated as described in example23.

TABLE 24 Xylose release from DFDSM using a GH11 xylanase (SEQ ID NO: 73)and four different GH62 arabinofuranosidases (SEQ ID NO: 21, 27, 45 or63) Conc. Conc. Percent [mg GH62 [mg Soluble solubi- GH11 EP/ Arabino-EP/ xylose lised Xylanase kg] furanosidase kg] (%) xylose¹ SEQ ID NO: 7310 None — 0.05 0.3 SEQ ID NO: 73 10 SEQ ID NO: 45 5 0.63 4.3 SEQ ID NO:73 10 SEQ ID NO: 27 5 0.43 3.0 SEQ ID NO: 73 10 SEQ ID NO: 21 5 0.39 2.7SEQ ID NO: 73 10 SEQ ID NO: 63 5 0.41 2.8 Table 24 shows the amount ofxylose measured after acid hydrolysis of supernatants (% of dry matterand % solubilized xylose of total xylose) when incubating DFDSM with SEQID NO: 73 (a GH11 xylanase) alone or in combination with a GH62arabinofuranosidase (SEQ ID NO 21, 27, 45 or 63). ¹Percentagesolubilised xylose was calculated as described in example 23.

TABLE 25 Xylose release from DFDSM using seven different GH11 xylanases(SEQ ID NO: 73, 74, 75, 78, 81, 88 or 89) and eight different GH62arabinofuranosidases (SEQ ID NO: 15, 18, 21, 24, 39, 51, 57 or 69) Conc.Conc. Percent [mg GH62 [mg Soluble solubi- GH11 EP/ Arabino- EP/ xyloselised Xylanase kg] furanosidase kg] (%) xylose¹ None — None — 0.01 0.0SEQ ID NO: 73 10 SEQ ID NO: 33 10 0.71 4.7 SEQ ID NO: 73 10 SEQ ID NO:39 10 1.05 7.0 SEQ ID NO: 73 10 SEQ ID NO: 51 10 1.05 2.5 SEQ ID NO: 7310 SEQ ID NO: 57 10 0.74 4.9 SEQ ID NO: 73 10 SEQ ID NO: 69 10 0.82 5.4None — None — 0.02 0.0 SEQ ID NO: 78 10 SEQ ID NO: 15 10 0.70 4.6 SEQ IDNO: 78 10 SEQ ID NO: 18 10 0.86 5.7 SEQ ID NO: 78 10 SEQ ID NO: 21 101.13 7.5 SEQ ID NO: 78 10 SEQ ID NO: 33 10 1.08 7.1 SEQ ID NO: 78 10 SEQID NO: 39 10 1.29 8.5 None — None — 0.01 0 SEQ ID NO: 74 10 SEQ ID NO:51 10 0.39 2.6 SEQ ID NO: 75 10 SEQ ID NO: 24 10 1.30 8.7 SEQ ID NO: 7510 SEQ ID NO: 51 10 0.41 2.7 SEQ ID NO: 81 10 SEQ ID NO: 24 10 1.49 10.0SEQ ID NO: 81 10 SEQ ID NO: 51 10 0.71 4.7 None — None — 0.01 0 SEQ IDNO: 87 10 SEQ ID NO: 24 10 1.37 9.2 SEQ ID NO: 87 10 SEQ ID NO: 51 100.42 2.8 SEQ ID NO: 88 10 SEQ ID NO: 51 10 0.30 1.9 SEQ ID NO: 89 10 SEQID NO: 51 10 0.35 2.3 Table 25 shows the amount of xylose measured afteracid hydrolysis of supernatants (% of dry matter and % solubilizedxylose of total xylose) when incubating DFDSM with a GH11 xylanase (SEQID NO: 73, 74, 75, 78, 81, 88 or 89) in combination with a GH62arabinofuranosidase (SEQ ID NO: 15, 18, 21, 24, 39, 51, 57 or 69).¹Percentage solubilised xylose was calculated as described in example23.

TABLE 26 Xylose release from DFDSM using two different GH11 xylanases(SEQ ID NO: 73 or 78) and eight different GH62 arabinofuranosidases (SEQID NO: 111, 117, 120, 129, 135 138, 144 or 147) Conc. Conc. Percent [mgGH62 [mg Soluble solubi- GH11 EP/ Arabino- EP/ xylose lised Xylanase kg]furanosidase kg] (%) xylose¹ None — None — 0.01 0.0 SEQ ID NO: 73 10 SEQID NO: 111 10 0.73 4.8 SEQ ID NO: 73 10 SEQ ID NO: 117 10 0.74 4.9 SEQID NO: 73 10 SEQ ID NO: 120 10 0.56 3.7 SEQ ID NO: 73 10 SEQ ID NO: 12910 0.71 4.7 SEQ ID NO: 73 10 SEQ ID NO: 135 10 0.55 3.7 SEQ ID NO: 73 10SEQ ID NO: 138 10 0.70 4.7 SEQ ID NO: 73 10 SEQ ID NO: 144 10 0.74 4.9SEQ ID NO: 73 10 SEQ ID NO: 147 10 0.69 4.6 None — None — 0.01 0.0 SEQID NO: 78 10 SEQ ID NO: 111 10 1.09 7.3 SEQ ID NO: 78 10 SEQ ID NO: 11710 1.18 7.9 SEQ ID NO: 78 10 SEQ ID NO: 120 10 0.93 6.2 SEQ ID NO: 78 10SEQ ID NO: 129 10 1.18 7.9 SEQ ID NO: 78 10 SEQ ID NO: 135 10 0.98 6.6SEQ ID NO: 78 10 SEQ ID NO: 138 10 1.19 8.0 SEQ ID NO: 78 10 SEQ ID NO:144 10 1.26 8.4 SEQ ID NO: 78 10 SEQ ID NO: 147 10 1.26 8.4 Table 26shows the amount of xylose measured after acid hydrolysis ofsupernatants (% of dry matter and % solubilized xylose of total xylose)when incubating DFDSM with a GH11 xylanase (SEQ ID NO: 73 or 78) incombination with a GH62 arabinofuranosidase (SEQ ID NO: 111, 117, 120,129, 135 138, 144 or 147). ¹Percentage solubilised xylose was calculatedas described in example 23.

TABLE 27 Xylose release from DFDSM using a GH11 xylanases (SEQ ID NO:99) and a GH62 arabinofuranosidases (SEQ ID NO: 24) Conc. Conc. Percent[mg GH62 [mg Soluble solubi- GH11 EP/ Arabino- EP/ xylose lised Xylanasekg] furanosidase kg] (%) xylose¹ None — None — 0.01 0.0 SEQ ID NO: 99 10None — 1.00 0.6 SEQ ID NO: 99 10 SEQ ID NO: 24 10 1.06 7.1 Table 27shows the amount of xylose measured after acid hydrolysis ofsupernatants (% of dry matter and % solubilized xylose of total xylose)when incubating DFDSM with SEQ ID NO: 99 (a GH11 xylanase) alone or incombination with a GH62 arabinofuranosidase (SEQ ID NO: 24).Conclusion

The results show that the percent solubilised xylose is significantlyhigher (at least 2 times) for the combinations of the GH11 xylanase andthe GH62 arabinofuranosidases tested compared to the GH11 xylanasealone.

Example 47: Hydrolysis of Defatted Destarched Maize (DFDSM) Using aCombination of a GH10 Xylanase and a GH62 Arabinofuranosidase

The experiment was performed as described in example 45 and the resultsare presented in tables 28 to 30 inclusive.

TABLE 28 Xylose release from DFDSM using three different GH10 xylanases(SEQ ID NO: 70, 71 or 72) and eight different GH62 arabinofuranosidases(SEQ ID NO: 24, 27, 45, 51, 57 or 69) Conc. Conc. Percent [mg GH62 [mgSoluble solubi- GH10 EP/ Arabino- EP/ xylose lised Xylanase kg]furanosidase kg] (%) xylose¹ None — None — 0.02 0.0 SEQ ID NO: 72 10 SEQID NO: 27 10 1.25 8.3 SEQ ID NO: 72 10 SEQ ID NO: 45 10 1.45 9.7 SEQ IDNO: 72 10 SEQ ID NO: 57 10 1.17 7.7 SEQ ID NO: 72 10 SEQ ID NO: 69 101.27 8.4 None — None — 0.02 0.0 SEQ ID NO: 70 10 SEQ ID NO: 24 10 0.503.2 SEQ ID NO: 70 10 SEQ ID NO: 51 10 0.36 2.3 SEQ ID NO: 71 10 SEQ IDNO: 24 10 1.82 12.2 SEQ ID NO: 71 10 SEQ ID NO: 51 10 1.19 7.9 Table 28shows the amount of xylose measured after acid hydrolysis ofsupernatants (% of dry matter and % solubilized xylose of total xylose)when incubating DFDSM with a GH10 xylanase (SEQ ID NO: 70, 71 or 72) incombination with a GH62 arabinofuranosidase (SEQ ID NO: 24, 27, 45, 51,57 or 69). ¹Percentage solubilised xylose was calculated as described inexample 23.

TABLE 29 Xylose release from DFDSM using two different GH10 xylanases(SEQ ID NO: 70 and 72) and eight different GH62 arabinofuranosidases(SEQ ID NO: 111, 117, 120, 129, 135 138, 144 or 147) Conc. Conc. Percent[mg GH62 [mg Soluble solubi- GH10 EP/ Arabino- EP/ xylose lised Xylanasekg] furanosidase kg] (%) xylose¹ None — None — 0.01 0.0 SEQ ID NO: 72 10SEQ ID NO: 111 10 0.93 6.2 SEQ ID NO: 72 10 SEQ ID NO: 117 10 1.02 6.8SEQ ID NO: 72 10 SEQ ID NO: 120 10 0.83 5.5 SEQ ID NO: 72 10 SEQ ID NO:129 10 1.17 7.8 SEQ ID NO: 72 10 SEQ ID NO: 135 10 0.91 6.1 SEQ ID NO:72 10 SEQ ID NO: 138 10 1.17 7.8 SEQ ID NO: 72 10 SEQ ID NO: 144 10 1.026.8 SEQ ID NO: 72 10 SEQ ID NO: 147 10 1.12 7.5 None — None — 0.00 0.0SEQ ID NO: 70 10 SEQ ID NO: 111 10 0.44 2.9 SEQ ID NO: 70 10 SEQ ID NO:117 10 0.39 2.6 SEQ ID NO: 70 10 SEQ ID NO: 120 10 0.39 2.6 SEQ ID NO:70 10 SEQ ID NO: 129 10 0.55 3.7 SEQ ID NO: 70 10 SEQ ID NO: 135 10 0.362.4 SEQ ID NO: 70 10 SEQ ID NO: 138 10 0.42 2.8 SEQ ID NO: 70 10 SEQ IDNO: 144 10 0.39 2.6 SEQ ID NO: 70 10 SEQ ID NO: 147 10 0.40 2.6 Table 29shows the amount of xylose measured after acid hydrolysis ofsupernatants (% of dry matter and % solubilized xylose of total xylose)when incubating DFDSM with a GH10 xylanase (SEQ ID NO: 70 or 72) incombination with a GH62 arabinofuranosidase (SEQ ID NO: 111, 117, 120,129, 135 138, 144 or 147). ¹Percentage solubilised xylose was calculatedas described in example 23.

TABLE 30 Xylose release from DFDSM using two different GH10 xylanases(SEQ ID NO: 102 and 180) and a GH62 arabinofuranosidase (SEQ ID NO: 24)Conc. Conc. Percent [mg GH62 [mg Soluble solubi- GH10 EP/ Arabino- EP/xylose lised Xylanase kg] furanosidase kg] (%) xylose¹ None — None —0.01 0.0 SEQ ID NO: 180 10 None — 0.64 4.2 SEQ ID NO: 180 10 SEQ ID NO:24 10 1.50 10.1 SEQ ID NO: 102 10 None — 0.11 0.7 SEQ ID NO: 102 10 SEQID NO: 24 10 0.75 5.0 Table 30 shows the amount of xylose measured afteracid hydrolysis of supernatants (% of dry matter and % solubilizedxylose of total xylose) when incubating DFDSM with SEQ ID NO: 102 or 180(a GH10 xylanase) alone or in combination with a GH62arabinofuranosidase (SEQ ID NO: 24). ¹Percentage solubilised xylose wascalculated as described in example 23.Conclusion

The results show that the percent solubilised xylose is significantlyhigher (at least 2 times) for all of the combinations of GH10 xylanaseand GH62 arabinofuranosidases tested compared to the GH10 xylanasealone.

Example 48: Hydrolysis of Defatted Destarched Maize (DFDSM) Using aCombination of a GH10 Xylanase and a GH62 Arabinofuranosidase

The experiment was performed as described in example 45 and the resultsare presented in table 31.

TABLE 31 Xylose release from DFDSM using a GH10 xylanases (SEQ ID NO:72) and ten different GH62 arabinofuranosidases (SEQ ID NO: 105, 123,153, 156, 159, 162, 165, 168, 171 or 174) Conc. Conc. Percent [mg GH62[mg Soluble solubi- GH10 EP/ Arabino- EP/ xylose lised Xylanase kg]furanosidase kg] (%) xylose¹ None — None — 0.005 0.0 SEQ ID NO: 72 10None 10 0.282 1.9 SEQ ID NO: 72 10 SEQ ID NO: 153 10 1.155 7.8 SEQ IDNO: 72 10 SEQ ID NO: 156 10 1.193 8.0 SEQ ID NO: 72 10 SEQ ID NO: 159 101.157 7.8 SEQ ID NO: 72 10 SEQ ID NO: 162 10 1.087 7.3 SEQ ID NO: 72 10SEQ ID NO: 165 10 1.077 7.2 SEQ ID NO: 72 10 SEQ ID NO: 168 10 0.986 6.6SEQ ID NO: 72 10 SEQ ID NO: 171 10 1.211 8.1 SEQ ID NO: 72 10 SEQ ID NO:174 10 1.071 7.2 SEQ ID NO: 72 10 SEQ ID NO: 105 10 1.268 8.5 SEQ ID NO:72 10 SEQ ID NO: 123 10 1.278 8.6 Table 31 shows the amount of xylosemeasured after acid hydrolysis of supernatants (% of dry matter and %solubilized xylose of total xylose) when incubating DFDSM with a GH10xylanase (SEQ ID NO: 72) in combination with a GH62 arabinofuranosidase(SEQ ID NO: 105, 123, 153, 156, 159, 162, 165, 168, 171 or 174).¹Percentage solubilised xylose was calculated as described in example23.Conclusion

The results show that the percent solubilised xylose is significantlyhigher (at least 2 times) for all of the combinations of GH10 xylanaseand GH62 arabinofuranosidases tested compared to the GH10 xylanasealone.

Example 49: Hydrolysis of Defatted Destarched Maize (DFDSM) Using aCombination of a GH11 Xylanase and a GH62 Arabinofuranosidase

The experiment was performed as described in example 45 and the resultsare presented in tables 32 to 34 inclusive.

TABLE 32 Xylose release from DFDSM using a GH11 xylanases (SEQ ID NO:78) and ten different GH62 arabinofuranosidases (SEQ ID NO: 105, 123,153, 156, 159, 162, 165, 168, 171 or 174) Conc. Conc. Percent [mg GH62[mg Soluble solubi- GH11 EP/ Arabino- EP/ xylose lised Xylanase kg]furanosidase kg] (%) xylose¹ None — None — 0.010 0.0 SEQ ID NO: 78 10None 10 0.352 2.3 SEQ ID NO: 78 10 SEQ ID NO: 153 10 1.165 7.8 SEQ IDNO: 78 10 SEQ ID NO: 156 10 1.148 7.7 SEQ ID NO: 78 10 SEQ ID NO: 159 101.085 7.3 SEQ ID NO: 78 10 SEQ ID NO: 162 10 1.183 7.9 SEQ ID NO: 78 10SEQ ID NO: 165 10 1.132 7.6 SEQ ID NO: 78 10 SEQ ID NO: 168 10 0.906 6.1SEQ ID NO: 78 10 SEQ ID NO: 171 10 1.118 7.5 SEQ ID NO: 78 10 SEQ ID NO:174 10 1.106 7.4 SEQ ID NO: 78 10 SEQ ID NO: 105 10 1.212 8.1 SEQ ID NO:78 10 SEQ ID NO: 123 10 1.172 7.9 Table 32 shows the amount of xylosemeasured after acid hydrolysis of supernatants (% of dry matter and %solubilized xylose of total xylose) when incubating DFDSM with a GH11xylanase (SEQ ID NO: 78) in combination with a GH62 arabinofuranosidase(SEQ ID NO: 105, 123, 153, 156, 159, 162, 165, 168, 171 or 174).¹Percentage solubilised xylose was calculated as described in example23.

TABLE 33 Xylose release from DFDSM using a GH11 xylanases (SEQ ID NO:73) and ten different GH62 arabinofuranosidases (SEQ ID NO: 105, 123,153, 156, 159, 162, 165, 168, 171 or 174) Conc. Conc. Percent [mg GH62[mg Soluble solubi- GH11 EP/ Arabino- EP/ xylose lised Xylanase kg]furanosidase kg] (%) xylose¹ None — None — 0.000 0.0 SEQ ID NO: 73 10None 10 0.059 0.4 SEQ ID NO: 73 10 SEQ ID NO: 153 10 0.894 6.0 SEQ IDNO: 73 10 SEQ ID NO: 156 10 0.777 5.2 SEQ ID NO: 73 10 SEQ ID NO: 159 100.695 4.7 SEQ ID NO: 73 10 SEQ ID NO: 162 10 0.709 4.8 SEQ ID NO: 73 10SEQ ID NO: 165 10 0.639 4.3 SEQ ID NO: 73 10 SEQ ID NO: 168 10 0.568 3.8SEQ ID NO: 73 10 SEQ ID NO: 171 10 0.654 4.4 SEQ ID NO: 73 10 SEQ ID NO:174 10 0.763 5.2 SEQ ID NO: 73 10 SEQ ID NO: 105 10 0.895 6.0 SEQ ID NO:73 10 SEQ ID NO: 123 10 0.892 6.0 Table 33 shows the amount of xylosemeasured after acid hydrolysis of supernatants (% of dry matter and %solubilized xylose of total xylose) when incubating DFDSM with a GH11xylanase (SEQ ID NO: 73) in combination with a GH62 arabinofuranosidase(SEQ ID NO: 105, 123, 153, 156, 159, 162, 165, 168, 171 or 174).¹Percentage solubilised xylose was calculated as described in example23.

TABLE 34 Xylose release from DFDSM using a GH11 xylanases (SEQ ID NO:96) and ten different GH62 arabinofuranosidases (SEQ ID NO: 105, 123,153, 156, 159, 162, 165, 168, 171 or 174) Conc. Conc. Percent [mg GH62[mg Soluble solubi- GH11 EP/ Arabino- EP/ xylose lised Xylanase kg]furanosidase kg] (%) xylose¹ None — None — 0.016 0.0 SEQ ID NO: 96 10None 10 0.198 1.2 SEQ ID NO: 96 10 SEQ ID NO: 153 10 1.153 7.7 SEQ IDNO: 96 10 SEQ ID NO: 156 10 1.108 7.4 SEQ ID NO: 96 10 SEQ ID NO: 159 101.037 6.9 SEQ ID NO: 96 10 SEQ ID NO: 162 10 1.020 6.8 None — None —0.014 0.0 SEQ ID NO: 96 10 None 10 0.200 1.2 SEQ ID NO: 96 10 SEQ ID NO:165 10 1.021 6.8 SEQ ID NO: 96 10 SEQ ID NO: 168 10 0.811 5.4 SEQ ID NO:96 10 SEQ ID NO: 171 10 0.933 6.2 SEQ ID NO: 96 10 SEQ ID NO: 174 100.994 6.6 SEQ ID NO: 96 10 SEQ ID NO: 105 10 1.025 6.9 SEQ ID NO: 96 10SEQ ID NO: 123 10 0.993 6.7 Table 34 shows the amount of xylose measuredafter acid hydrolysis of supernatants (% of dry matter and % solubilizedxylose of total xylose) when incubating DFDSM with a GH11 xylanase (SEQID NO: 96) in combination with a GH62 arabinofuranosidase (SEQ ID NO:105, 123, 153, 156, 159, 162, 165, 168, 171 or 174). ¹Percentagesolubilised xylose was calculated as described in example 23.Conclusion

The results show that the percent solubilised xylose is significantlyhigher (at least 2 times) for all of the combinations of GH11 xylanaseand GH62 arabinofuranosidases tested compared to the GH11 xylanasealone.

Example 50: Determination of Hydrolysis of Arabinoxylans in Corn andWheat DDGS Substrate

Corn DDGS from a European corn-based fuel ethanol plant was used assubstrate (93.35% dry substrate). Wheat DDGS from a European wheat-basedfuel ethanol plant was used as substrate (92.43% dry substrate) The DDGSwas ground in a coffee blender for 3-4 minutes and washed extensively inwater (six times, each wash followed by centrifugation at 3000 rpm for15 minutes) to remove soluble dry matter.

After the repeated washings the amount of dry substrate (DS) wasmeasured and a 15% DS slurry in water was prepared for the trial andadjusted to pH 4.8 using 1M NaOH.

Enzymes

The enzymes used were the GH10 xylanase from Aspergillus aculeatus (SEQID NO: 72) and the GH62 arabinofuranosidase from Penicillium capsulatum(SEQ ID NO: 9).

Assay

4 g slurry was transferred to a PCR-tube plate. Sodium azide (0.05%) andenzyme (see table 30) was added each well. The plate was covered with amanual plate-sealer and the samples were incubated for 24 hours at 40°C. and 500 rpm, with samples taken after 0 and 24 hours. The sampleswere boiled for 10 minutes to deactivate the enzymes, centrifuged andfiltered (0.2 μm filter).

TABLE 35 Experimental design and enzyme doses Dose (μg e.p./ TestSubstrate Enzyme g DS) Repeats 1 Wheat DDGS Blank  0 2 2 Wheat DDGS GH10 (SEQ ID NO: 72) 30 2 3 Wheat DDGS GH 62 (SEQ ID NO: 9) 30 2 4 WheatDDGS GH 10 (SEQ ID NO: 72) + 20 + 10 2 GH 62 (SEQ ID NO: 9) 5 Wheat DDGSGH 10 (SEQ ID NO: 72) + 15 + 15 2 GH 62 (SEQ ID NO: 9) 6 Wheat DDGS GH10 (SEQ ID NO: 72) + 30 + 30 2 GH 62 (SEQ ID NO: 9) 7 Corn DDGS Blank  02 8 Corn DDGS GH 10 (SEQ ID NO: 72) 30 2 9 Corn DDGS GH 62 (SEQ ID NO:9) 30 2 10 Corn DDGS GH 10 (SEQ ID NO: 72) + 20 + 10 2 GH 62 (SEQ ID NO:9) 11 Corn DDGS GH 10 (SEQ ID NO: 72) + 15 + 15 2 GH 62 (SEQ ID NO: 9)12 Corn DDGS GH 10 (SEQ ID NO: 72) + 30 + 30 2 GH 62 (SEQ ID NO: 9)Analytical Methods

1. Brix Measurements

The soluble dry substance (Brix) was measured using a Mettler ToledoBrix meter.

2. Absorption at 320 nm

Adsorption at 320 nm was measured after 50× dilution with water.Adsorption at 320 nm is a measure of the soluble fragments containingferulic acid. The assay was calibrated with a ferulic acid standard(A320 (OD)=0.0147+0.0628*[concentration of ferulic acid in μg/ml])

3. Xylose (for 24 Hour Samples)

Xylose content was determined using the “D-xylose assay kit” fromMegazymes.

Results

TABLE 36 Soluble dry matter as determined using the Brix measurementSample 1 Sample 2 Test Substrate/enzyme 0 hours (mg/mL) (mg/mL) 1 Wheat,blank 0.99 1.26 1.4 2 Wheat, GH10 0.99 2.03 2.1 3 Wheat, GH62 0.99 1.541.4 4 Wheat, GH10 + GH62 0.99 1.96 2.23 5 Wheat, GH10 + GH62 0.99 1.962.23 6 Wheat, GH10 + GH62 0.99 2.17 2.17 7 Corn, blank 0.43 0.64 0.64 8Corn, GH10 0.43 1.2 1.2 9 Corn, GH62 0.43 0.71 0.71 10 Corn, GH10 + GH620.43 1.61 1.68 11 Corn, GH10 + GH62 0.43 1.75 1.68 12 Corn, GH10 + GH620.43 1.75 1.82

TABLE 37 Amount of soluble fragments containing ferulic acid measured byadsorption at 320 nm Sample 1 Sample 2 Test Substrate/enzyme 0 hours(mg/mL) (mg/mL) 1 Wheat, blank 0.163 0.258 0.328 2 Wheat, GH10 0.1630.347 0.378 3 Wheat, GH62 0.163 0.215 0.261 4 Wheat, GH10 + GH62 0.1630.354 0.424 5 Wheat, GH10 + GH62 0.163 0.359 0.421 6 Wheat, GH10 + GH620.163 0.368 0.375 7 Corn, blank 0.027 0.043 0.047 8 Corn, GH10 0.0270.279 0.287 9 Corn, GH62 0.027 0.061 0.047 10 Corn, GH10 + GH62 0.0270.432 0.456 11 Corn, GH10 + GH62 0.027 0.504 0.475 12 Corn, GH10 + GH620.027 0.510 0.534

TABLE 38 Xylose release from DDGS Sample 1 Sample 2 TestSubstrate/enzyme 0 hours (mg/mL) (mg/mL) 1 Wheat, blank 1.38 1.56 1.73 2Wheat, GH10 1.38 5.57 6.00 3 Wheat, GH62 1.38 1.67 1.77 4 Wheat, GH10 +GH62 1.38 5.44 6.09 5 Wheat, GH10 + GH62 1.38 6.17 5.55 6 Wheat, GH10 +GH62 1.38 5.71 5.91 7 Corn, blank 0.06 0.13 0.12 8 Corn, GH10 0.06 2.492.47 9 Corn, GH62 0.06 0.37 0.34 10 Corn, GH10 + GH62 0.06 4.50 4.35 11Corn, GH10 + GH62 0.06 4.50 4.30 12 Corn, GH10 + GH62 0.06 4.16 4.63

It is concluded from the data in this example that for wheat DDGS, theGH10 xylanase (SEQ ID NO: 72) is able to fully degrade the substrate andthe addition of a GH62 arabinofuranosidase does not give any additionalrelease of xylose.

For corn DDGS the GH10 xylanase alone (SEQ ID NO: 72) is unable to fullydegrade the substrate. However, when the GH62 arabinofuranosidase (SEQID NO: 9) is added, the release of xylose is significantly improved.This example clearly shows the difference between the less substitutedwheat based substrate and highly substituted corn based substrate andthat the combination of a GH10 xylanase and GH62 arabinofuranosidase issignificantly better than a GH10 xylanase alone on corn basedsubstrates.

What is claimed is:
 1. A composition comprising a GH10 polypeptidehaving xylanase activity at least 85% sequence identity to thepolypeptide of SEQ ID NO: 70, and a GH62 polypeptide havingarabinofuranosidase activity and at least 85% sequence identity to thepolypeptide of SEQ ID NO: 12, wherein: (a) the GH10 polypeptide and theGH62 polypeptide together solubilise at least 2.0% xylose from defatteddestarched maize (DFDSM); and (b) the GH10 polypeptide and the GH62polypeptide together solubilise at least 2 times more xylose from DFDSMthan the GH10 polypeptide in the absence of the GH62 polypeptide;wherein (a) and (b) are performed under the reaction conditions: (i) 25mg GH10 polypeptide per kg DFDSM, (ii) 12.5 mg GH62 polypeptide per kgDFDSM, and (iii) incubation at 40° C., pH 5 for 4 hours.
 2. Thecomposition of claim 1, wherein the GH10 polypeptide has at least 90%sequence identity to the polypeptide of SEQ ID NO: 70, and the GH62polypeptide has at least 90% sequence identity to the polypeptide of SEQID NO:
 12. 3. The composition of claim 1, wherein the GH10 polypeptidehas at least 95% sequence identity to the polypeptide of SEQ ID NO: 70,and the GH62 polypeptide has at least 95% sequence identity to thepolypeptide of SEQ ID NO:
 12. 4. The composition of claim 1, whereinGH10 polypeptide has at least 346 amino acid residues and has xylanaseactivity, and the GH62 polypeptide has at least 273 amino acid residuesand has arabinofuranosidase activity.
 5. The composition of claim 1,wherein the GH10 polypeptide has at least 85% sequence identity to thepolypeptide of SEQ ID NO: 70 with one or more amino acid substitutions,deletions and/or insertions to the polypeptide of SEQ ID NO: 70, and theGH62 polypeptide has at least 85% sequence identity to the polypeptideof SEQ ID NO: 12 with one or more amino acid substitutions, deletionsand/or insertions to the polypeptide of SEQ ID NO:
 12. 6. Thecomposition of claim 1, wherein the GH10 polypeptide comprises SEQ IDNO: 70, and the GH62 polypeptide comprises SEQ ID NO:
 12. 7. An animalfeed additive comprising the composition of claim 1 and one or morecomponents selected from the list consisting of: one or more vitamins;one or more minerals; one or more amino acids; and one or more otherfeed ingredients.
 8. An animal feed comprising the composition of claim1 and plant-based material from the sub-family Panicoideae.
 9. A methodof improving one or more performance parameters of an animal comprisingadministering to one or more animals the composition of claim
 1. 10. Amethod of solubilising xylose from plant based material, comprisingtreating plant based material from the sub-family Panicoideae with thecomposition of claim
 1. 11. A method of releasing starch from plantbased material, comprising treating plant based material from thesub-family Panicoideae with the composition of claim
 1. 12. A method forimproving the nutritional value of an animal feed, comprising adding tothe feed the composition of claim
 1. 13. A method of preparing an animalfeed, comprising mixing the composition of claim 1 with plant basedmaterial from the sub-family Panicoideae.